Molecular B2 Flashcards

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1
Q

Transcription
Carbs
Replication
Ucc stuff

A
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2
Q

UCC
Proteins are composed of amino acids. How many amino acids are there?
How are different proteins made?
How are proteins made?
How does RNA polymerase know where to start from?

A

20 amino acids
Different proteins are made by combining these 20 amino acids in different combinations

Step 1- transcription
Part of DNa temporarily unzips and is used as a template to assemble complementary nucleotides into messenger RNA(mRNa)
Nucleotides are added into a complimentary strand of mRNa based on the DNA code
This mRNa strand leaves the nucleus and goes to the ribosome for translation

Translation steps:
mRNaa is read by rRNA
rRNa makes up the ribosome

mRNa is read three bases at a time
Every three bases on mRNa codes for one amino acid and is called a codon
A codon refers to three bases on mRNa that codes for one amino acid
Amino acids are brought until the entire mRNa is read.
Each tRNA drops off one amino acid then goes into the cytoplasm to grab another
The Ribosome bonds each amino acid together using a peptide bond creating a polypeptide
Eventually the stop codon is reached and the final amino acid is added

It knows because mRNa has a start codon which is a specific three letter nucleotide sequence that says begin here
The start codon on mRNA is the three letters AUG
Remember how big DNA is
The entire molecule is not used to make mRNa just a small portion
Stop codon tells RNA polymerase to stop making the protein

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3
Q

UCC
What is cellular reproduction specifically binary fission and give examples of organisms that reproduce by binary fission
Give types of binary fission

A

From 1 cell to 2 cells
Example Amoeba,bacteria,euglena,paramecium
So I’m binary fission the DNA undergoes replication and then cytokinesis into two identical daughter cells
Binary fission is a type of asexual reproduction
The prokaryotic chromosome duplicates or replicates
There is continued cell growth
Cells divide into two identical daughter cells
Prokaryotes have cell wall

Longitudinal binary fission:divides the cells into left and right
Transverse binary fission :divide into up and down
Irregular binary fission

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4
Q

UCC
Explain the cell cycle

A cell cycle is thus a sequence of events that a cell goes through as it grows and divides to produce new cells. Therefore, it can be called the life cycle of a cell.
True or false
Chromosome is made up of DNA which is made up of a gene true or false
A single chromosome has a chromatid and a centromere
A duplicated chromosome has sister chromatids and a centromere true or false
What’s a homologous chromosome
What is an allele?
What is meiosis
What’s the difference between meiosis I and meiosis II
Explain how meiosis occurs
Explain the role of growth factors in cell cycle

A

Gnot or G subscript 0 is the phase where there is cell cycle arrest
G1 the cellular contents excluding the chromosomes are duplicated or there hs cell growth
S phase each of the 46 chromosomes is dubplicated by the cell or there is DNA replication
G2 phase the cell “double checks” the duplicated chromosomes for error making any needed repairs or there’s progressive mitosis

All true
A homologous chromosome are chromosomes that all have the same genes in the same places along their length

An allele is different forms of chromosome on the same gene

Meiosis takes place only in the reproductive cell types (sperm and egg cells) of sexually reproducing organisms, including humans. For a cell to undergo meiosis, it must have a diploid (2n) chromosome number.

In meiosis I, a pair of homologous chromosomes separate to produce two diploid daughter cells, each having half the number of chromosomes as the parent cell. In contrast, during meiosis II, sister chromatids separate to produce four haploid daughter cells. Also, unlike meiosis I, no genetic recombination by crossing over occurs in meiosis II.

Interphase :
Cell replicates it’s chromosomeS
Each chromosome has two sister chromatids held together by a centromere

Prophase 1:
Chromosome could up and a spindle forms
Homologous chromosomes come together to form a tetrad
Crossing over May occur resulting in variations

Metaphase 1:
Centromere of each chromosome becomes attached to a spindle fiber
Spindle fibers pull the tetrads to the equator of the spindle
Homologous chromosomes line up side by side as tetrads

Anaphase 1:
Homologous chromosomes separate and move to opposite ends of the cell
Centromeres do not split
This ensures that each new cell will receive only one chromosome from each homologous pair

Telophase 1:
Spindle breaks down and chromosomes uncoil
Cytoplasm divides to yield two new cells
Each cell has half the genetic information of the original cell because it has only one homologous chromosome

Prophase II:
A spindle forms in each of the two new cells and fibers attach to the chromosomes

Metaphase II:
The chromosomes line up randomly at the equator

Anaphase II:
The centromere of each chromosome splits
The sister chromatids separate and move to opposite poles

Telophase II
Nuclei are formed
Spindles break down
The cytoplasm divides (cytokinesis)

Meiosis II is identical to mitosis

Growth factors such as serum are hugely specific proteins required in very low concentrations for effective running of the cell cycle
It is known that cultured cells deprived of serum stop proliferating and arrest in Gnot or G0

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5
Q

Ucc
Explain how mitosis occurs in the cell cycle
What checkpoints are there in the cell cycle

Ucc
What are labile cells,stable cells,permanent cells
What is quiescence

A

A eukaryotic cell cycle consists of two main parts: 1) interphase and 2) mitotic (M) phase, and an alternative part called the G0-phase.

1) Interphase

It is the first phase of the cell cycle, recognized by the growth period where the chromosome gets duplicated as the cell prepares for division. Interphase happens between one cell division or mitotic (M) phase and the next. It is the longest part of the cell cycle involving three sub-phases. The typical duration of this phase is 23 hours.

G1-phase: Also known as the first-gap phase, during this period, the cells grow in size, synthesize cell organelles and other macromolecules such as proteins that serve as the building block of the cell. The cells also accumulate sufficient energy required for division.
S-phase: Also known as the synthesis phase, the existing DNA is copied within the nucleus. This process of DNA synthesis is also known as DNA-replication. The centrosome is also duplicated during this phase and gives rise to spindle fibers. The entire S-phase requires energy expenditure to proceed.
G2-phase: This is the second gap phase and is somewhat similar to the G1-phase. During this period, the cells grow further in size, making more proteins and organelles. All preparations for mitosis get completed before the cells enter the mitotic phase.
2) Mitotic (M) Phase

This period is also known as the cell division phase and occurs just after the G2-phase. Here, the cell divides its genetic material (DNA) and cytoplasm to form two new cells. The M-phase involves two different critical processes that unfold in the following order:

a) Mitosis or Karyokinesis

It is the nuclear division period and consists of four phases: prophase, metaphase, anaphase, and telophase. During this phase, the cell divides the nucleus and gets separated into two daughter cells, where each daughter cell receives a complete set of chromosomes. The details of its different phases are discussed in the mitosis article.

b) Cytokinesis

It is the process by which the cytoplasm of the cell splits to form two independent cells. The phase of cytokinesis begins towards the end of mitosis such that the two processes overlap. Cytokinesis is the shortest phase of the cell cycle that occurs differently in plants and animals.

The division in plant cells occurs by forming a cell plate structure in the middle of the cell. The cell plate is made of components made of the cell membrane and cell wall.
The division in animal cells happens when a band of cytoskeletal fibers known as contractile rings forms just below the cell membrane in the metaphase plate’s position. The contractile rings contract inwards, thus creating a depression or crack, called cleavage furrow. The cracks increase, and slowly the membrane cleaves to form two daughter cells at the end of the cell cycle.
End Result

Two individual daughter cells are formed, each having identical copies of the genetic material.

G0-phase

Some cells do not immediately enter another round of preparatory phase or interphase following the division or mitosis. Instead, they exit the G1 growth phase and enter a resting stage called G0-phase. Thus, G0 is also called the alternative phase of the cell cycle. Some cells enter the G0-phase temporarily until an outside signal triggers the onset of G1. In contrast, other cells that either never divide or seldom divide, such as nerve cells or cardiac cells, remain in G0-phase permanently.

The main checkpoints are:

  1. G1-checkpoint: Present just before the entry into S-phase, it makes the critical decision whether the cell will enter the S-phase. The decision is based on whether the cell is big enough and has synthesized proteins necessary for DNA synthesis.
  2. G2-checkpoint: Checks errors in the DNA-synthesis phase and, based on the result, bars the entry into the M-phase. This checkpoint helps to prevent the occurrence of cancer in higher animals. Suppose there is an error in DNA replication. In that case, the G2 checkpoint prevents the cell from progressing further in the cell cycle and checks the error in the newly formed DNA.
  3. M-checkpoint: This occurs near the end of the metaphase stage. It checks whether all sister chromatids are correctly attached to the spindle fibers. The M-checkpoint ensures that equal division of chromosome occurs between the two daughter cells.

In cellular biology, labile cells are cells that continuously multiply and divide throughout life. This continual division of labile cells allows them to reproduce new stem cells and replace functional cells that are lost in the body
Example hematopoietic stem cells

Labile cells multiply continuously, and are found in bone marrow, various tissues, skin, and in the linings of most hollow organs in the body. Stable cells only multiply when needed or if another cell is destroyed or damaged, and are found in the liver and many other glands.

In cellular biology, stable cells are cells that multiply only when needed. They spend most of the time in the quiescent G0 phase of the cell cycle but can be stimulated to enter the cell cycle when needed. Examples include the liver, the proximal tubules of the kidney and endocrine glands.

3) the permanent cells, incapable of multiplication in the adult—only the permanent cells are incapable of regeneration. These are the brain cells and the cells of the skeletal and heart muscles.

Quiescence is the reversible state of a cell in which it does not divide but retains the ability to re-enter cell proliferation. Some adult stem cells are maintained in a quiescent state and can be rapidly activated when stimulated, for example by injury to the tissue in which they reside

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6
Q
Ucc
What are Carbohydrates 
State the classification of carbs
How are monosaccharides classified ?
What are enantiomers
State the differences between D and L sugars
A

They contain element sCHo and the chem structure is C6H12O6

Monosaccharides:cannot be hydrolysis further into smaller units
Disaccharides
Polysaccharides

Carbs usually end with the suffix -Ose
Example gluc-Ose,malt-Ose,cellul-Ose

Monosaccharides are classified based on the number of carbon atoms

Number of carbon atoms:3
Type of monosaccharides is triose

4-tetrose
5-pentose
6-hexose

They are also classified according to the type of carbonyl group they contain
Example:aldehyde=Aldose:aldohexose
Ketone=ketose:ketohexose

There are two simple classes of the carbonyl group: Aldehydes and Ketones. Aldehydes have the carbon atom of the carbonyl group is bound to a hydrogen and ketones have the carbon atom of the carbonyl group is bound to two other carbons.1

Those monosaccharides that contain an aldehyde functional group are called aldoses; those containing a ketone functional group on the second carbon atom are ketoses.
To understand better,look at the structure of glucose and fructose and see the difference
Use this link https://chem.libretexts.org/Courses/Sacramento_City_College/SCC%3A_Chem_309_-General_Organic_and_Biochemistry(Bennett)/Text/14%3A_Carbohydrates/14.2%3A_Classes_of_Monosaccharides

Thus, monosaccharides are described as aldotetroses, aldopentoses, ketopentoses, ketoheptoses, and so forth. Glucose and fructose are specific examples of an aldohexose and a ketohexose, respectively

So monosaccharides can only be classified as either aldoses or ketoses then you add the number of carbons

Molecules that are nonsuperimposable (nonidentical) mirror images of each other are a type of stereoisomer called enantiomers (Greek enantios, meaning “opposite”).

a) D- and L-glyceraldehyde are mirror images of each other and represent a pair of enantiomers

Sugars whose Fischer projections terminate in the same configuration as D-glyceraldehyde are designated as D sugars; those derived from L-glyceraldehyde are designated as L sugars. The main difference between D and L Glucose is that D-Glucose rotates plane polarized light clockwise whereas L-Glucose rotates plane polarized light anticlockwise. The main difference between L and D isomers is that the OH- group of the penultimate carbon is positioned on the right side of the D isomer whereas, in L isomer, it is located on the left side. D-Glucose is the enantiomer of L-Glucose, for example.

D sugars-dextrorotatory
L-levorotatory
Look at pictures of l and d sugars

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7
Q

UCc:
What is stereogenecity or stereogenic/chiral Centre
Give examples of Naturally occuring D sugars
Look at pictures of stereogenic centers in the examples of naturally occuring D sugars

A

The ability of a C atom to exhibit enantiomerism

An atom, or a grouping of atoms, is considered to be a stereogenic center if the interchange of two ligands attached to it can produce a new stereoisomer. All chiral centers are stereogenic centers but all stereogenic centers are not chiral centers.23 Jun 2017

Stereo center is a point in a molecule which can give rise to stereoisomers. Chiral center is a carbon atom to which four different atoms or groups of atoms are bonded. Nature. A stereocenter is a point in a molecule, not necessarily an atom. A chiral center is a carbon atom.

D -fructose
D-glucose
D-ribose
D-glyceraldehyde

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8
Q

Ucc:
Explain ring formation and mutarotation: alpha and beta forms
Give examples

A

Mutarotation is the change in the optical rotation because of the change in the equilibrium between two anomers, when the corresponding stereocenters interconvert. Cyclic sugars show mutarotation as α and β anomeric forms interconvert.

When β-D-glucopyranose is dissolved in water, it rotates a plane-polarized light by +18.7°. Some amount of β-D-glucopyranose undergoes mutarotation, to give α-D-glucopyranose and it turns a plane-polarized light by +112.2°.

The mutation occurs when the anomeric position (C1) changes its configuration between α and β form in the solution. As a result, carbohydrates undergo ring-opening to form hemiketal (aldehyde form) and reforms into a hemiacetal (closed ring).

The mutation occurs when the anomeric position (C1) changes its configuration between α and β form in the solution. As a result, carbohydrates undergo ring-opening to form hemiketal (aldehyde form) and reforms into a hemiacetal (closed ring).

Alpha is better for humans and beta is better for animals (ruminants)

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9
Q

Ucc:
What are disaccharides
Explain anomerism or acetal or hemiacetal formation in disaccharide

Why is it that reducing sugars can be metabolized in humans, but non-reducing sugars cannot?

Difference between acetal / hemiacetal formation or anomerism

Explain pyrans and furans and give examples

Difference between alpha anomers and beta anomers with regards to cis and trans

A

Two monosaccharides: glucose + glucose = maltose
Glucose + fructose= sucrose
Glucose + galactose = lactose

C-1 of glucose become chrial carbon and has two possible arrangements of H and OH group around itThese two arrangements of glucose which differ only in the orientation of hydroxyl group at C-1 are called anomers. Eg:- α-D-Glucose and β-D-Glucose.

We can conclude that the Sucrose is not a reducing sugar because it does not have a hydroxyl group in the ring. Hence, sucrose does not show mutarotation. All other disaccharides are reducing sugars

Because reducing sugars can open their cyclic structure into the straight chain form, whereas non-reducing sugars cannot

Explanation:
When it comes to metabolizing sugars, only reducing sugars are able to undergo breakdown. This is because reducing sugars are able to be converted from their closed chain form into their open chain form. It is only in the open chain form that sugars such as glucose can be metabolized.

Only reducing sugars can be converted into their open chain form. The reason for this is that the anomeric carbon for these sugars is not occupied

Anomers are cyclic monosaccharides or glycosides that are epimers, differing from each other in the configuration of C-1 if they are aldoses or in the configuration at C-2 if they are ketoses. The epimeric carbon in anomers are known as anomeric carbon or anomeric center.

Example 1: α-D-Glucopyranose and β-D-glucopyranose are anomers.

Hemiacetal is formed as an intermediate product between acetal formation. Hemiacetal and acetal are acknowledged as functional groups. The critical difference between hemiacetal and acetal is that hemiacetal contains one -OH and one -OR group while acetal contains two -OR groups.

Acetal: Acetal is a group of atoms that is represented by a central carbon atom bonded to two –OR groups, -R group and a –H group. Hemiacetal: Hemiacetal is a group of atoms composed of a central carbon atom bonded to four groups; an –OR group, -OH group, -R group and a –H group.

Where R is the carbon group

furanose compounds have a chemical structure that includes a five-membered ring system containing four carbon atoms and one oxygen atom whereas pyranose compounds have a chemical structure that includes a six-membered ring structure consisting of five carbon atoms and one oxygen atom.

Aqueous glucose-pyranose
Aqueous fructose- furanose

the research group of Walter Haworth, who conclusively determined that the hexose sugars preferentially form a pyranose, or six-membered, ring. Haworth drew the ring as a flat hexagon with groups above and below the plane of the ring – the Haworth projection.

When an open chain monosaccharides cyclizes to a furanose or pyramids form,a new stereogenic center is formed at what used to be the carbonyl carbon.
The two stereomers produced are called Anomers and the hemi-acetal carbon atom is called an anomerism Centre

Alpha-anomer (α-anomer): A carbohydrate in which the group bonded to the anomeric carbon is trans to the CH2O group on the other side of the pyranose or furanose ring ether oxygen atom. In α-D-glucopyranose the anomeric OH is trans to the CH2OH. In β-D-glucopyranose the anomeric OH is cis to the CH2OH.

The key difference between alpha and beta anomers is that in alpha anomer, the hydroxyl group at the anomeric carbon is cis to the exocyclic oxygen at the anomeric centre, whereas in beta anomer, the hydroxyl group is trans to the exocyclic oxygen.

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10
Q

Ucc:
What’s the structural importance of polysaccharides
What do Aldoses react with tk yield oxidized sugars?
Why are Aldoses reducing sugars?

A

Cell walls
Chitin : a fibrous substance consisting of polysaccharides, which is the major constituent in the exoskeleton of arthropods and the cell walls of fungi.

Lignin : a complex organic polymer deposited in the cell walls of many plants, making them rigid and woody.

Polysaccharides are complex sugars example amylase,cellulase,starch

Aldoses react with Tollen’s,Fehling’s,Benedict’s reagents to yield oxidized sugars

They are reducing sugars because the sugar reduces the oxidizing agent
Some diabetic test kits use Benedict’s test that gives a reddish precipitate as a positive sign

Other oxidizing agents include the earth metals example formic acid,oxalic acid and sulphite compounds

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11
Q

Ucc:
What is an epimer,a carbonyl group,furanose,pyranose,glycoprotein,glycoside formation,acetal,
What are the two kinds of starch,what’s the major difference between amylose and amylopectin,what’s the basic chemical difference between starch and cellulose,what’s the chemical nature that makes it impossible for humans to digest cellulose,what’s the biological nature of humans that makes it impossible to digest cellulose,what is cellobiose,partial hydrolysis of cellulose?
What are glycosides,homoglycans,heteroglycans,epimerism,enolization,oxazone,proteiglycan,Pataus syndrome,klinefelters syndrome

A

Epimer:one of a pair of stereoisomers that differ in configuration at only one stereogenic Centre

Carbonyl group: a carbon atom with a. Double bond to oxygen and a single bond to hydrogen atoms or alkyl group

Furanose: five members cyclic hemiacetal structure

Pyranose: six membered rings

Glycoprotein:
Carbohydrate with a protein part (conjugated protein)

Glycoside formation: reaction of monosaccharides with alcohol with and acid catalyst. They form glycosidic linkages
Acetal: a functional group consisting of two ether type oxygen atoms bound to the same carbon

Types of starch:

Starch consists of glucose molecules. It can occur in two forms: amylose and amylopectin. Amylose is a linear or straight-line polymer that scientists describe as amorphous or solid. Amylopectin forms a branched chain and is crystalline. Or The main difference between amylose and amylopectin is that amylose is a straight chain polymer whereas amylopectin is a branched chain polymer
Amylopectin is more in starch than amylose and is more soluble in water than amylose and it forms a gel wben hot water is added and the amylose doesn’t do that

Starch and cellulose: There is only one difference. In starch, all the glucose repeat units are oriented in the same direction. But in cellulose, each succesive glucose unit is rotated 180 degrees around the axis of the polymer backbone chain, relative to the last repeat unit. Starch contains alpha glucose, while cellulose is made of beta glucose

The presence of beta acetal linkages in cellulose makes it different from starch and is a deciding factor in its digestibility. Humans lack the enzyme required to break down the linkages.

Humans can digest starch but not cellulose because humans have enzymes that can hydrolyze the alpha-glycosidic linkages of starch but not the beta-glycosidic linkages of cellulose.

The reason is due to the different types of bonding between cellulose and starch. Cellulose has beta-1,4 bonds that are not digested by our enzymes (which can digest alfa-1,4 and alfa-1,6 bonds that are present in starch and glycogen).

The key difference between cellobiose and cellulose is that cellobiose is a disaccharide, whereas cellulose is s polysaccharide. Moreover, cellobiose is a reducing sugar while cellulose is a non-reducing sugar.

Definition of cellobiose
a faintly sweet disaccharide C12H22O11 obtained by partial hydrolysis of cellulose.

Glycosides are naturally occurring substances composed of a sugar that is linked to another functional group via a glycosidic bond. They are colorless, amorphous, solid, non-volatile compounds. They give a positive test with Molisch and Fehling’s solution test. They have solubility in water but are insoluble in organic solvents.

The glycosidic bond joining these two components is usually through an oxygen (O), sulfur (S) or a nitrogen atom (N).

Homoglycan: A polysaccharide is called a homoglycan when it contains only one type of monosaccharide unit, for example, cellulose,glycogen are all composed of glucose subunits .A large number of plant products belong to this particular category, namely, honey, starch,

Heteroglycan: A polysaccharide is known as a heteroglycan when it involves more than one kind of monosaccharide unit, for example, d-gluco-d-mannose is made up of d-glucose and d-mannose.

Epimers are carbohydrates which vary in one position for the placement of the -OH group. The best examples are for D-glucose and D-galactose

Epimerization is a process in stereochemistry in which there is a change in the configuration of only one chiral center. As a result, a diastereomer is formed. The classical example of this in medicine is tetracycline.

Enolization or a keto-enol-tautomerism is a process of converting a ketone kr an aldehyde to a corresponding enol (in acidic conditions) or an enolate (in basic conditions)
An enol is an organic compound that contains a hydroxyl group bonded to a carbon atom having a double bond and that is usually characterized by the grouping C=C(OH)

Osazone test is a chemical test used to detect reducing sugars. This test even allows the differentiation of different reducing sugars on the basis of the time of appearance of the complex. This test is also termed Phenyl hydrazine test based on the reagent used for this test.

Osazones are a class of carbohydrate derivatives found in organic chemistry formed when reducing sugars are reacted with excess of phenylhydrazine at boiling temperatures

glycoprotein:
any of a class of proteins which have carbohydrate groups attached to the polypeptide chain. lycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Example of glycoproteins are antibodies 

There are three types of glycoproteins based on their structure and the mechanism of synthesis: N-linked glycoproteins, O-linked glycoproteins, and nonenzymatic glycosylated glycoproteins. Glycoproteins are always found on the outside of the plasma membrane, with the sugar facing out.

Proteoglycans are glycosylated proteins which have covalently attached highly anionic glycosaminoglycans.

in proteoglycans, one or more glycosaminoglycan chains are attached to the protein while in glycoproteins, oligosaccharide chains are attached to proteins. The largest in size and most abundant by weight is aggrecan, a proteoglycan

Patau syndrome: A condition in which a person has an extra chromosome 13.

Patau syndrome is the result of trisomy 13, meaning each cell in the body has three copies of chromosome 13 instead of the usual two. The most common cause is nondisjunction of chromosome 13 during meiosis.

Klinefelter syndrome
Also called: XXY syndrome
A genetic condition in which a male is born with an extra copy of the X chromosome
Due to maternal nondisjunction cases are caused by meiosis I errors,

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12
Q

Ucc:
Explain the history of cells
Explain the cell theory
Cells must’ve able to divide,they vary in size and shape,some cells are organisms onto themsekves(unicellular example bacteria) and they’re the simplest form of life. Others only fu croon when they ar w part of a large organisms (multicellular) such as cells making up the human body true or false
The nucleus and cytoplasm is made up of?
Give some examples of membranous organelles and define them

Give some examples of non membranous organelles and define them

Is the cell wall membrane bound or non membrane bound

What are the characteristic of the nucleus
State the types of cells and state the charac of prokaryotic cells and eukaryotic cells

A

In the 17 th century 1670,Robert Hooke upon examining cork with a microscope observed that it was made of tiny chambers.
With his knowledge of small rooms or chambers found in monasteries at that time called in Latin Cella,he names these chambers cells
Similar compartments were seen in animal tissue

In 1838,Schleiden and Schwann: hypothesized that all plant and animal tissues were made up of cells
Robert Remak and Rudolf Virchow: how are living things reproduced?
All organisms are composed of one or more cells
The cell is the basic building block of all organisms
Cells arise form pre existing cells

Cells were then deemed the ultimate units of living organisms because cells are the smallest potential Independent unit of a living organism
Later,cells were found to contain smaller structures such as nucleus in their cytoplasm

Nuclear envelope
Chromatin
Nucleolus

Cytoplasm:
Inclusions(non living cytoplasmic materials . Structures not usually surrounded by a plasma membrane example lipids,glycogen,pigment granules) and organelles(little organs. A specialized sub unit within a cell that has a specific function. Types of organelles include membranous or membrane limited compartments and non membranous example microtubules

Membranous organelles:
Plasma(cell) membrane:
A lipid bilayer that forms the cell boundary and boundaries of many organelles in the cell

Rough surfaced endoplasmic reticulum:
Associated with ribosomes and site of protein synthesis and modification of newly synthesized proteins

Smooth surfaced endoplasmic reticulum:
Involves in lipid and steroid synthesis

Golgi apparatus:
Has multiple flattened cisternae for modifying,sorting and packaging proteins and lipids for intracellular or extracellular transport

Endosomes:
Sorting proteins delivers to them via endocytotic vessels and redirecting them to different cellular compartments for their final destination

Lysosomes:
Contain digestive enzymes,digest invaders,breakdown of old cell parts.

Mitochondria:
Provision of most energy to the cell by producing adenosine triphosphate (ATP) in the process of oxidative phosphorylation

Peroxisomes: degradation of molecules like fatty acids,amino acids and foreign substances

Non membranous organelles:
Microtubules- form part of the cytoskeleton and continuously elongate( by adding Tubulin dimers ) and shorten

Ribosomes: responsible for protein synthesis and composed of ribosomal RNA

Filaments: form part of the cytoskeleton and are of actin filaments and intermediate filaments

The organelles that are non-membranous include ribosomes, the cytoskeleton, the cell wall, centrosomes, and the centrioles. These organelles are not contained by a membrane, unlike membrane-bound organelles.

The nucleus is the most prominent organelle in the eukaryotic cell
It’s a double membrane structure and contains the genetic information of the cell and contains the chromosomes and nucleolus(direct synthesis of RNA and forms ribosomes)

Prokaryotes: capsule,cell wall,plasma membrane,cytoplasm,ribosomes,plasmid,pill
Prokaryotes don’t have a nucleus,are spherical,rod like shaped and small,presence of cell wall,simple and limited in structure,have circular or linear DNA,has nucleoid that is a region of DNa concentration and is lived mostly as a single celled organism but some join to form chains or clusters or other organized multicellular structures example bacteria,archaea

Spiral shape: treponema pallidum,
Rod shaped: escherichia coli
Spherical:streptococcus

Eukaryotes: possess nucleus,have organelles and other sub cellular structures
Bigger and more elaborate ,some live as independent and singe celled organisms such as amoebae and yeast
Example yeast,fungus,protozoan,plant and animal

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13
Q

What are the types of biological molecules
Name the four types of non covalent or weak interactions among bio molecules in aqueous solvent

Weak interactions are crucial to macromolecular structure & function true or false

A

Types of biological molecules
– Proteins (all synthesized from the same 20 species of amino acids)
– Nucleic acids (made from 8 types of nucleotides) – Polysaccharides (made from 8 commonly
occurring types of sugars)
– Lipids (made up of alcohols and fatty acids)

Hydrogen bonds between neutral groups and between peptide bonds
Ionic interactions:attraction and repulsion
Hydrophobic interactions
Van der Waals

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14
Q

What is the formula for pH?
Name four acidic and neutral and basic examples
Why is pH important and what happens if it alters?

Weak Acids are the acids that do not completely dissociate into their constituent ions when dissolved in solutions.

What’s the pH of trypsin
What the relationship between acid,Ka and pKa
State the Henderson-Hasselbalch equation
What’s the use of this equation
When will pH be equal to pKa

A

pH+pOH=14
pOH= -log[OHraised to the power -]

Acidic:lemon juice,gastric juice,black coffee,milk,saliva,beer,tomato juice,vinegar,red wine

Basic:seawater,egg white,household bleach and household ammonia,solution of baking soda

What happens if it alters?
E.g. Blood pH constant at ~7.4
– If pH <7.3 CO2 not removed from cells—– acidosis
– In severe diabetes, pH can fall to 6.8 coma and death
Intracellular pH ~7.4
– Enzymes and metabolic processes sensitive to pH
– How is pH maintained? Neutral solution pH is 7
Not an arbitrary number Derived from ionic product of water

Neutral:human blood and tears (pH of 7 is neutral)

Trypsin:around 6,
Pepsin: around 2

Weak acids and bases have characteristic dissociation constants:
CH3COOH can dissociate to form CH3COO- + H+

HA can dissociate to form A- + H+

Keq = [A-] [H+] divided by [HA] = Ka(dissociation constant)

K_a	=	acid dissociation constant
[A^-]	=	concentration of the conjugate base of the acid
[H+]	=	concentration of hydrogen ions
[HA]	=	concentration of chemical species HA

pKa= -logKa = log

1 divided by Ka

Stronger the acid ,Higher the Ka ,Lower the pKa

pH=pKa + log [A raised to the power -] / [HA]

The Henderson-Hasselbach equation is used to
• Calculate pKa, given pH and molar ratio of proton donor and acceptor
• Calculate pH, given pKa and molar ratio of proton donor and acceptor
• Calculate the molar ratio of proton donor and acceptor, given pH and pKa
pH= pKa+ log
[proton acceptor] / [proton donor]
When [proton acceptor] = [proton donor], pH= pKa

When [A]=[HA] or at the midpoint of titration then pH=pKa

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15
Q

Explain buffers

Buffers work from 1 pH unit below to 1 pH unit above. So if the pKa is 4.76, the buffering region will be between 5.76-3.76
their pKa true kr false

A

Buffers
• Buffers are solutions that resist changes in pH as acid and base are added
• Most buffers consist of a weak acid and its conjugate base
• Note in titration figure how the plot of pH versus base added is flat near the pKa
• Buffers can only be used reliably within a pH unit of their pKa

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16
Q

How many sugars do the chains of the types of carbohydrates contain
State the functions of carbs
State the types of carbs
Monosaccharides under organic chemistry can be classified into what and what?

A

Monosaccharide (1)
Oligosaccharide (2-20)
Polysaccharide (>20)

Main role of “carbo” (Carbohydrates) in nature 􏰀 Storage of energy
􏰀 Structural support
􏰀 Lipid and protein modification
􏰀 recognition by IgG
􏰀 /cell cell communication
Carbohydrates are hydrates of carbon
Chemical composition (C . H2O)n n>3
• Monosaccharides (simple sugars)
• Oligo = "a few" - usually 2 to 10
• Polysaccharides are polymers of the simple sugars

Types
Carbohydrates
• Monosaccharides (simple sugars)
• Disaccharides
• Oligosaccharides(short-chain carbohydrates)
• Polysaccharides (long chain carbohydrates)

Monsaccharides
An organic chemistry review
• Aldoses and ketoses contain aldehyde and ketone functions, respectively
• Triose, tetrose, etc. denotes number of carbons
• Aldoses with 3C or more and ketoses with 4C or more are chiral

polyhydroxy: Aldehydes Ketones are aldoses are
ketoses
Number of carbons:
3=triose 4=tetrose 5=pentose 6=hexose

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17
Q

What’s re the types of monosaccharides with regards tk the number of carbons and with regards to polyhydroxyl

Look at examples of stereoisomers of glyceraldehyde and how they differ r

A

Triose - Smallest monosaccharide
Has three carbon atoms Tetrose (4C)
Pentose (5C) Hexose (6C) Heptose (7C) etc…

Name :triose -Formula-
C3 H6 O3 
tetrose -formula-C4 H8 O4
pentose-formula-C5 H1 0 O5
hexose-C6 H1 2 O6
heptose -C7 H1 4 O7
octose-C8 H1 6 O8

Aldoses (e.g., glucose) have an aldehyde group at one end

Ketoses (e.g., fructose) have a keto group, usually at C2

Aldehydes and Ketones. Both aldehydes and ketones contain a carbonyl group, a functional group with a carbon-oxygen double bond.

Propanal is an example of an aldehyde functional group. R−CHO is a general structural formula for Aldehyde.

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18
Q

What are enantiomers
What does D mean in D aldoses
What are epimers and give example
Cyclic form of glucose and fructose is called?
Read about what ucc talked about concerning carbs

A

Mirror image configurations(read UCc definition)

D-aldoses
D refers to configuration at chiral center most distance
from carbonyl carbon

Two Sugars that only differ in configuration around one carbon atom

Cyclic monsaccharide structures and anomeric forms
• Glucose (an aldose) can cyclize to form a cyclic hemiacetal
• Fructose (a ketose) can cyclize to form a cyclic hemiketal
• Cyclic form of glucose is a pyranose • Cyclic form of fructose is a furanose

Cyclization leads to pair of diasteromers known as anomers
• Hemiacetal or the hemiketal C is known as
• For D-sugars, alpha has OH down, beta up

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19
Q

What are reducing sugars
Why do ketoses act as reducing sugars
Sugars on mild reaction produce what?

A

Monosaccharide Derivatives
• Reducing sugars: sugars with free anomeric carbons - they will reduce oxidizing agents, such as peroxide, ferricyanide and some metals (Cu and Ag)
• These redox reactions convert the sugar to a sugar acid
• Glucose is a reducing sugar - so these reactions are the basis for diagnostic tests for blood sugar

Sugars as reducing agents
(Ketoses isomerize to aldoses under the conditions used for these oxidation reactions with copper ions and thus also act
as reducing sugars.)

Produce sugar alcohol

Example sorbitol,mannitol and xylitol
Used to sweeten sugarless food products

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20
Q

Name three important monosaccharides and why they’re important
What are disaccharide
Give examples
What links two monosaccharides?

A

Important monosaccharides
• Glucose - Aldose. Preferred source of energy for brain cells and cells without mitochondria
• Fructose – ketose. Sperm use this as major sugar/energy source for motility
• Galactose - important for lactose (milk sugar) production

Disaccharide - two monosaccharides linked together
Linked via a glycosidic linkage
• Examples:
– Sucrose (table sugar) : • Glucose + fructose
– Maltose:
• Glucose + Glucose
– Lactose (milk sugar) : • Glucose + Galactose

  This ring can’t open up and is no longer reducing This ring can open up to an aldehyde and is still reducing

Sugars bearing anomeric C that has not formed glycosidic bonds are called reducing sugars
Because they reduce mild oxidizing agents

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21
Q

Why can’t people hydrolyze lactose ?
Take note of this: Oligosaccharides and other carbs
Don’t memorize structures, but know the important features
• Be able to identify anomeric carbons and reducing and nonreducing ends
• Sucrose is NOT a reducing sugar
• Note carefully the nomenclature of links! Be able to recognize alpha(1,4), beta(1,4), etc

A

Hydrolysis of dietary Lactose
• Some people don’t produce enough lactase, the enzyme that hydrolyzes lactose, and so can’t digest lactose
• Many adults become lactose intolerant

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22
Q

What are polysaccharides
State functions
What’s their nomenclature

A

Polysaccharides
(also known as glycans)
Functions: storage, structure, recognition
• Nomenclature: homopolysaccharide vs. heteropolysaccharide(look at the difference on the slides)
• Starch and glycogen are storage molecules
• Chitin and cellulose are structural molecules
• Cell surface polysaccharides are recognition molecules

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23
Q

What are structural polysaccharides

What’s the model of cellulose

A

Structural Polysaccharides
Composition similar to storage polysaccharides, but small structural
differences greatly influence properties
• Cellulose is the most abundant natural polymer on earth
• Primary structural component of plant cell walls
• Cellulose can also be soft and fuzzy - in cotton
• Linear polymer of up to 15,000 D-glucose residues

Model of Cellulose
Highly cohesive, H-bonded structures give cellulose
fibers exceptional strength & make them water
insoluble despite their hydrophilicity

Wood and bark are insoluble formed from cellulose

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24
Q

What are the forms of starch
Which is more abundant
Why us there branching in starch

A

Starch
A plant storage polysaccharide
Polymer of D - glucose
• Two forms: amylose and amylopectin
• Most starch is 10-30% amylose and 70-90% amylopectin
• Branches in amylopectin every 12-30 residues (branch is 1,6 link)
• Amylose has alpha(1,4) links, one reducing end

Why branching in Starch?
Consider the phosphorylase reaction…
• Phosphorylase releases glucose-1-P products from the amylose or amylopectin chains
• The more branches, the more sites for phosphorylase attack
• Branches provide a mechanism for quickly releasing (or storing) glucose units for (or from) metabolism

25
Q

What is glycogen

A

Glycogen
The glucose storage device in animals
• Glycogen constitutes up to 10% of liver mass and 1-2% of muscle mass
• Glycogen is stored energy for the organism
• Only difference from starch: number of branches
• Alpha(1,6) branches every 8-12 residues (amlyopectin 12-30)
• More branched than amylopectin
• Glycogen gives a red-violet color with iodine
Photomicrograph showing the glycogen granules (pink) of a liver.
Glycogen content of liver may reach 10% of its net weight

Bacteria cell wall consists of covalently linked polysaccharide & polypeptide chains

26
Q

What are lipids
What are the functions of lipids
Classification of lipids

A

What are Lipids? (Greek: lipos, fat)
• Fourth major group of molecules found in cell
• Lipids are not polymeric
(unlike nucleic acids, proteins & polysaccharides)
• Water insoluble
(soluble in organic solvents such as methanol & chloroform)
• Includes fats, oils, certain vitamins and hormones

Lipids of biological importance
Major functions:
1. They serve as structural components of biological membranes
2. Energy reserve, predominantly in the form of triacylglycerols
3. Both lipids and lipid derivatives serve as vitamins, hormones, signalling molecules
4. Bile acids aid in lipid solubilization

Lipid Classification

  1. Fatty acids
  2. Triacylglycerols
  3. Glycerophospholipids
  4. Sphingolipids
  5. Steroids
  6. Other lipids (Example: Eicosanoids)
27
Q

What are membranes made of

What are fatty acids

A
What are membranes made of?
Biological membranes are composed of proteins associated with a lipid bilayer matrix
 Oligosaccharide
Lipid (bilayer)
Protein
Cholesterol

Oleic acid has a double bond on the 9 th carbon
Alpha linolenic acid has the double bond on the 9,12th,15th carbons

Fatty Acids
o Carboxylic acids with long hydrocarbon side group (R-COOH) o Usually occur in esterified form (R-COOR)
o Can be either saturated or unsaturated (contain double bonds) o Often are polyunsaturated (2 or more double bonds)
o Double bonds have cis configuration and are non conjugated

28
Q

Explain Packing of fatty acids into stable aggregates

Melting point of fatty acid increases with what? Give examples

A

Packing of fatty acids into stable aggregates
Pack Efficiently
Stabilized by hydrophobic interactions
Presence of one or more cis double bonds interferes with tight packing
Results in less stable aggregate

Melting points of fatty acids
􏰀 Increase with increase in chain length (or molecular mass) For Example:
Melting Point (oC)
12(chain length):0( Lauric acid 44.2 (melting point)
18(chain length):0 Stearic acid 69.1
􏰀 Decrease with the degree of unsaturation (or increase in double bonds)
For Example:
Melting Point (oC)
18:0 Stearic acid 69.1
18:1 Oleic acid 13.2
18:2 Linoleic acid -9

29
Q

What are essentially fatty acids and non essential
Give examples
What are waxes and give examples

A

Essential fatty acids - linoleic and linolenic are two examples of essential fatty acids
Non- Essential fatty acids
those that can be synthesized in the body
Linolenic acid
18:3Δ9,12,15
Essential fatty acid: An omega-3 polyunsaturated fatty acid

Position of the first site of unsaturation relative to the omega end of that fatty acid

Waxes
• Waxes are esters of long chain (C14-C36) saturated and unsaturated fatty acids with long chain (C16-C30) alcohols.

30
Q

What are triglycerides
Why are fats a good way to store metabolic energy
Explain the principal class of storage of and membrane lipids

A

Triacyl Glycerols (triglycerides)
􏰁 Fatty acid triesters of glycerol
􏰁 Non polar, water insoluble
􏰁 Fats & oils are mixtures of triacyl glycerol
􏰁 Function as energy reservoirs in animals
􏰁 Usually not part of biological membranes
Fats are good way to store metabolic energy
􏰀More energy than sugars or proteins which are partially oxidized
􏰀Fats are non-polar and are stored in anhydrous form (unlike glycogen which binds twice its weight of water)

Storage lipids (neutral):triglycerides (glycerol plus three fatty acids)
Membrane lipids(polar):phospholipids( divided into glycerophospholipids(glycerol plus two fatty acids ,alcohol and phosphate(PO4-) )and sphingolipids(sphingosine plus fatty acid ,choline and phosphate(PO4-) )and glycolipids (divided into sphingolipids(sphingosine plus fatty acid and mono or oligosaccharide )
31
Q

What are the characteristic of Glycerophospholipids
Give three examples
What are Sphingolipids
What are The Common Classes of Glycerophospholipids.

A

Glycerophospholipids (or phosphoglycerides) as a
Major lipid components of biological membranes

1.Derived from glycerol-3-phosphate whose C1 and C2 positions are esterified with fatty acids
2.Phosphoryl group is linked to a group “X”
3.Amphiphilic molecule:
non-polar hydrocarbon tail
polar phosphoryl X “heads”

Eg. Phosphatidylethanolamine Phosphatidylserine
Phosphatidylcholine Phosphatidylinositol phosphatidylglycerol

Sphingolipids:
􏰂Major membrane components 􏰂Derived from C18 amino
alcohol, sphingosine 
􏰂Double bond of sphingosine
has trans configuration
32
Q

What is plasmalogen
What are sphingolipids
What are steroids and their functions

Cholesterol is a 27 carbon compound with a unique structure with a hydrocarbon tail, a central sterol nucleus made of four hydrocarbon rings, and a hydroxyl group. The center sterol nucleus or ring is a feature of all steroid hormones. True or false

Steroids are oxidized derivatives of sterols. Name four steroids derived from cholesterol

A

Plasmalogen
􏰂 Glycerophospholipids
􏰂 At C1 position there is a, b-unsaturated ether linkage instead of ester linkage
􏰂 Functions of most plasmalogen not well understood
Choline
From Lehninger
Principles of Biochemistry
Ethanolamine, choline & serine form the most common plasmalogen head groups

Sphingolipids
􏰂Major membrane components 􏰂Derived from C18 amino
alcohol, sphingosine 􏰂Double bond of sphingosine
has trans configuration

Steroids
􏰁 Structure consists of three 6-membered rings & one 5-membered ring, all fused together
􏰁 Cholesterol is the most common steroid in animals (& precursor for all other steroids in animals)
􏰁 Steroid hormones serve many functions in animals - including salt balance, metabolic function and sexual function

Testosterone,cortisol,prednisolone,prednisone,aldosterone,Estradiol

33
Q

What are unsaturated fatty acids and Eicosanoids
What are inflammatory bio molecules ?
Give five examples
Where are they made
What’s their half-life
What are they made from?
What are the classical inflammation response

A

UNSATURATED FATTY ACIDS AND EICOSANOIDS
• Dietary intake of certain polyunsaturated fatty acids
derived from a plant source is necessary •
• These essential fatty acids give rise to eicosanoic (C20) fatty acids, from which are derived families of compounds known as eicosanoids

Eicosanoids
• Prostaglandins
• Thromboxanes
• leukotrienes

Inflammatory Biomolecules
Signal Molecules:
– Histamine

– Eicosanoids
• Prostaglandins
• Thromboxanes
• Leukotrienes

– Bradykinins

– Cytokines
• Interferons
• Interleukins
• Chemotaxins
– Other minor molecules...
• Made in almost all tissues • Very short half-life
• Act locally on neighbors
• Not usually stored up
• 20-carbon backbones
• Made from arachidonic acid
Symptoms:
Redness
Swelling
Heat or fever
Pain
34
Q

Why study protein structure?
What’s the classification of amino acids
State each classes characteristics and give examples

A

Structure helps us understand function
The structure determines the function
Disruption of structure causes disruption of function Many disorders are due to aberrant protein structure
Example SCD

Classification of amino acids
Amino acids are classified based on properties of their R groups
Classification
1. amino acids with non-polar (hydrophobic) side chains
2. amino acids with polar, uncharged side chains 3. amino acids with polar, charged side chains

  1. Amino acids with non-polar, hydrophobic side chains
    R characteristics:
    •Unable to bind or give off protons •No hydrogen bonding
    •No ionic bonding
    •Participate in hydrophobic interactions
    Examples:glycine,alanine,proline,valine,methionine,leucine,isoleucine,phenylalanine,tryptophan

Amino acids with uncharged, polar side chains. Examples -tyrosine,serine,glutamine,cysteine,threonine,Asparagine

  1. Amino acids with polar, charged side chains R characteristics:
    • R group is charged at pH 7 (R+ or R-)
    • Sub-groups:
    Amino acids with R+ : basic Amino acids with R- : acidic
• Acidic
 – R group = carboxylic acid
– Donates H+
– Negatively charged 
Example aspartate and glutamate 
• Basic
– R group = amino
– Accepts H+
– Positively charged
Example lysine,arginine,histidine
35
Q

Under ionic forms of glycine,what is isoelectric point

Overview of protein structure
1. Numerous conformations of a protein are possible (without breaking a bond, by just rotation about single bonds)
2. However, a conformation existing under a given condition is the most stable thermodynamically, having the lowest Gibbs free energy
3. Proteins in any of their functional folded conformations are called native protein
True or false
Explain the structure of a peptide bond

A

Ionic forms of Glycine
pI - the pH at which the net charge on Glycine is zero
pI – isoelectric point

The peptide bond is rigid and planar
O
C = N 1.27 Ao C N 1.47 Ao
􏰀 6 atoms lie in a single plane
􏰀 Oxygen atom of the carbonyl group & the H of
amide nitrogen are in trans
􏰀 Bond between C and N has double bond character
and is unable to rotate
􏰀 Rotation is permitted between N – Ca and Ca – C
􏰀 Polypeptide backbone: series of rigid planes with
consecutive planes sharing a common point of rotation at Ca.
The carbonyl oxygen has a partial negative charge and the amide nitrogen a partial positive charge,
setting up a small electric dipole. Virtually all peptide bonds are planar and have this trans
configuration

36
Q

Explain the levels of structure in proteins
What’s the use of the primary structure?
Give two examples

A

Primary structure:made of amino acid residues . Linking of amino acids
• Linear sequence of amino acids linked together by peptide bonds
• Unique for each protein

Secondary structure:alpha helix. Stable arrangement of amino acids give rise to structural patterns.
Tertiary structure:made of polypeptide chains. 3-dimensional folding of polypeptides
Quaternary structure :made of assembled sub units of polypeptides
Arrangement in space of 2 or more polypeptide subunits

Primary structure: useful in detecting amino acid substitutions/replacements
e.g.
Conservative substitution: substitution of an amino acid with another of similar character/polarity
Gly-Ser-Val-Trp-Lys-Val-Asp-Arg (normal)
Gly-Ser-Val-Phe-Lys-Val-Asp-Arg

Non-conservative substitution: substitution of an amino acid with another of different character or polarity
Arg-Asp-Lys-Glu-Phe-Gly-Gly-His (normal)
Arg-Asp-Lys-Val-Phe-Gly-Gly-His

37
Q

Explain the secondary structure of proteins and the characteristics of the types
Explain the interactions between R groups of amino acid sequence 3 residues apart in a helix

A

Protein Secondary Structure
􏰁 Refers to the local conformation of some part of polypeptide
􏰁 Prominent secondary structures that are stable and occur in proteins are
1) a helix: —– Shows the hydrogen bonds. 1. f = -57o
2. y = -47o
3. Each helical turn includes 3.6 AA
4. a helix found in all proteins is
right handed

a helix 1. Forms readily

  1. Helical structure is very stable due to internal hydrogen bonds
  2. Between H attached to N of peptide linkage & the electronegative carbonyl O of the 4th AA on the N-terminal side of the peptide bond
  3. Within the helix, every peptide bond participates in such H bonding (except the last 4 amino acids that are close to the end of the helix)

2) b conformation: The b conformation of the polypeptide chains
The backbone of the polypeptide chain is extended into a zigzag structure
Zigzag structures arranges side by side to form a structure resembling a series of pleats (called b sheet)
Hydrogen bonds cross-links between adjacent chains

Interactions:

  1. AA sequence affects helix stability
  2. For example, polypeptide with long block of Glu residues will not form an a helix at pH 7
  3. Bulk shape of Cys, Ser, Thr can destabilize the helix if they are close together in a chain
  4. Proline introduces destabilizing kink in a helix
  5. Gly occurs infrequently as it is very flexible & takes coiled structure different from a helix
38
Q

Explain the structure of silk
What is the beta turn
What type is more common

A

Structure of silk
Silk or spider web made up of the protein fibroin.
It has Layers of antiparallel b sheet
Each chain of fibroin is made up of multiple repeats of the sequence (Gly-Ser-Gly-Ala-Gly-Ala)n.
Small R groups allow close packing

The Beta Turn (aka beta bend, tight turn)
• •

Allows the peptide chain to reverse direction
Carbonyl C of one residue is H-bonded to the amide proton of a residue three residues away
Proline & glycine are prevalent in beta turns
Type I is more common

39
Q

Proteins are classified into three major groups
Name em
Explain the relationship between protein structure and biological function

A

Proteins are classified into 3 major groups:
A. Globular proteins
• Polypeptide folded into globular shape, compact
• Contain more than 1 type of secondary structure
• Hydrophobic interior, hydrophilic surface
• Globular proteins include enzymes, transport and regulatory protein
• Soluble in water
B. Fibrous proteins
• Polypeptide chain arranged in sheets or strands
• Contain single type of secondary structure
• Often assembled into long filaments/ cables or threads
• Insoluble in water
C. Membrane proteins

Secondary structure and properties of fibrous protein
Structure: alpha Helix cross linked by disulfide bonds
Characteristics:tough ,insoluble,protective structures of varying hardness and flexibility
Examples of occurrence:alpha keratin of hair,feathers and nails

Structure : beta conformation
Characteristics:soft,flexible filaments
Example of occurrence:Silk fibroin

Structure:collagen triple helix
Characteristics:high tensile strength,without stretch,
Examples of occurrence:collagen of tendons,bone matrix

40
Q

What are fibrous proteins
What is collagen
What’s alpha keratin.

A hair is an array of many a-keratin filaments. What are the filaments?

A

Fibrous proteins: Provide mechanical support Often assembled into large cables or threads
α-Keratins: major components of hair and nails
Collagen: major component of tendons, skin, bones

Filaments(from cross section of hair):cells-intermediate filament-protofibril-protofilament-two chained coil-alpha helix

41
Q

State the constituents of collagen

What are the characteristics of collagen

A

Collagen has a distinct tertiary and quaternary structure
• Collagen is 35% Gly
11% Ala
21% Pro and Hyp
(Hyp is 4-hydroxyproline)
•Repeating tripeptide sequence Gly-X-Y, where X is often Pro and Y is often Hyp
•Unique secondary structure distinct from a helix
•Adopts a left-handed helical structure with three residues per turn
•Forms a three-stranded superhelix •Gelatin is derived from collagen

42
Q

Name four diseases,their protein deposits,the toxic protein,disease genes and the risk factors
Look at the slide with it for the rest

A

Alzheimer’s:extracellular plaques :A beta:APP,presenilin 1 and 2: apoE4 allele
Alzheimer’s:intracellular tangles:tau:

Parkinson’s:lest bodies:alpha Synuclein:alpha synuclein,Parkin,UCHL 1:tau linkage

43
Q

What is the tertiary structure of proteins and state the characteristics of tertiary structure

What holds a protein’s tertiary structure together ?

A

Tertiary structure
Describes the shape of completely folded polypeptide chain (functional protein)
Most stable conformation (structure) of a protein
Example: Myoglobin

characteristic:
Interaction between R groups
Amino acids that are far apart
in the primary structure are brought close enough to have side
chain interactions

What holds a protein’s tertiary structure together ?
• Disulfide bonds between side chain of Cys residues
[-S-S-] it’s Strong; confers a certain amount of rigidity
Disulfide bond
Form between two intra- or inter-chain Cys residues Product called Cystine
Stabilizes protein

• Hydrophobic interactions (between R groups of
non-polar amino acids), Hydrogen bonding between R groups

.Weak: • Ionic interactions/electrostatic interactions or “salt bridges”
Moderate strength

44
Q

Explain quartenary structure
Sub units in this structure are stabilized by what?
What is flexibility?

A

Quaternary structure
Arrangement of two or more polypeptide chains into a functional protein (multi-subunit) , e.g. Hb(hemoglobin. It has 4 sub units. Two alpha and two beta)
Subunit: a single polypeptide chain Each subunit has a tertiary
structure
Subunit – functional ????

Subunits: may be identical or different
Association of subunits – unique feature of quaternary structure of proteins

Subunits: stabilized by weak interactions
Stabilization by weak interactions confers flexibility
Flexibility, i.e. allows conformational /structural changes (within the same protein, e.g. Hb)

45
Q

What is the native state of protein
Explain denaturation of a protein and it’s effects on the protein and give examples of denaturating products
Explain renaturation of protein

A

Native state of a protein
A protein folded to form its tertiary/quaternary structure is said to be in its native state
Native state – most stable conformation of a protein
Native protein – functional

Denaturation of a protein - Unfolding a protein
Protein denaturation results in the unfolding and disorganization of a protein’s secondary, tertiary and quaternary structure
Denaturation:
Disruption of bonds/interactions stabilizing protein

Denaturation: not strong enough to break the peptide bonds
Primary structure remains intact after denaturation
Denaturation of a protein results in loss of function or reduced activity
Examples:heat,alcohol,acids and bases,heavy metals,reducing agents
Denaturation causes the protein to be in no specific shape

Renaturation
Refolding of protein to regain biological activity/function
Only few proteins can undergo renaturation

46
Q

Name six protein functions

A
Protein Functions
• ENZYMES
• Structural support (e.g. Collagen)
• Transport(e.g.Hemoglobin): O2 binding and transport: Hemoglobin and Myoglobin
A classic model of protein function
Red blood cells (erythrocytes)
 ~34% by weight hemoglobin (Hb)
• Immunity (e.g. Antibodies)
• Movement (e.g. myosin in muscles cells)
•Receptorproteins(e.g.rhodopsinineyes)
• Regulatory(e.g.hormones)
47
Q

What is myoglobin
Explain its structure
What is heme. Explain its characteristics
What’s the colour of venous blood,arterial blood,old meat

A

Myoglobin
• Small intracellular protein in vertebrate muscle
• Oxygen binding protein
• Globular protein
• First protein whose structure was determined by X-ray crystallography
• 153 residues
• 8 a helices
• Heme is tightly wedged in a hydrophobic pocket between the E and F helices

Myoglobin Structure
Mb is a monomeric heme protein
• Mb polypeptide “cradles” the heme group
• Fe in Mb is Fe2+ - ferrous iron - the form that
binds oxygen
• Oxidation of Fe yields 3+ charge - ferric iron - metmyoglobin does not bind oxygen
• Dioxygen binds as the sixth ligand to Fe

  • facilitates dioxygen transport in muscle and NO metabolism
  • 153 amino acid residues • 8 a-helical segments, A-H
  • His93 (proximal histidine) binds directly to iron
  • No other covalent attachments of heme to protein (contrast cytochrome c)
  • Globin – means without heme

Heme
• is a prosthetic group
•is permanently associated with the protein’s native structure & function
• consists of a protoporphyrin ring bound to ferrous iron ( Fe2+)
• the iron has six coordination bonds, four to nitrogens within the ring and two perpendicular to the ring
• heme is noncovalently bound to protein (Fe-N bond is a coordinate covalent bond)

DeoxyHb His-Fe2+ (color of venous blood)
OxyHb His-Fe2+-O2 (color of arterial blood)
MetHb His-Fe3+-OH2 (color of old meat)
MetHb does not bind dioxygen.
Water occupies the 6th coordination site
48
Q

Explain the myoglobin oxygen binding curve
What’s gives rbcs their colour
What is hemoglobin
What does the S shaped curve of Hb permit?

CO2 (high in tissues) is also carried by hemoglobin
This reaction produces protons and additional salt bridges stabilize the T state. True or false

A

Mb saturated with oxygen
Rectangular hyperbola
• Curve shape typical of the simple binding of a small molecule to a protein
• at very low pO2, very little O2 binds to Mb • at very high pO2, Mb is saturated with O2

Hb
• Intracellular protein that gives red blood cells their color
• Not just a simple O2 tank
• Sophisticated delivery system that provides the proper amount of oxygen to tissues under variety of circumstances
• Tetramer

Tertiary structure of a globin and beta globin are remarkably similar both to each other and to Mb
Only 18% of the corresponding residues are identical among these 3 polypeptides

Hb – sigmoidal (S-shaped curve)
This permits the blood to deliver much more O2 to the tissue than if Hb had a hyperbolic curve with the same P50

In any binding system, a sigmoidal curve is diagnostic of a cooperative interaction between binding sites
Binding of one dioxygen molecule increases the affinity of Hb for binding additional dioxygen molecules.

49
Q

What is special about 2,3-BPG (2,3-bisphosphoglycerate)
BPG in blood is normal what concentration
Why is BPG called an allosteric effector

A
2,3-BPG and Hb
The "inside" story......
• Wheredoes2,3-BPGbind?
 – "Inside"
– in the central cavity
• What is special about 2,3-BPG?
– Negative charges interact with 2 Lys, 4 His, 2 N- termini
• FetalHb-loweraffinityfor2,3-BPG,higher affinity for oxygen, so it can get dioxygen from
mother

BPG binds in central cavity
• BPG decreases dioxygen binding affinity of Hb
• Preferentially binds to deoxy state
• BPG binding to deoxyHb is ionic in character
• BPG shifts the T R equilibrium towards the T state
hence lower affinity for dioxygen

BPG binding stabilizes the T state of deoxyHb

BPG in blood normally 5 mM, but it rises at high altitudes
An Allosteric Effector of Hemoglobin
• In the absence of 2,3-BPG, oxygen binding to Hb follows a rectangular hyperbola!
• The sigmoid binding curve is only observed in the presence of 2,3-BPG
• Since 2,3-BPG binds at a site distant from the Fe where oxygen binds, it is called an allosteric effector

50
Q

What causes Sickle cell anemia

A

Sickle-Cell Anemia
There are over 300 variants of Hb. 95% of the variants differ by only a single amino acid in the primary sequence of either the alpha or beta chain of Hb.
Sickle-cell anemia is caused by a mutant form of hemoglobin, called HbS. HbS contains a single Glu to Val change at amino acid number six in the beta chain.
10% of African Americans are heterozygotic for HbS.
Subtle difference in surface charge in beta chain creates a hydrophobic patch in the HbS protein.

Protein Aggregation
The substitution of Val for Glu at postion 6 in the two b-chains causes the deoxyhemoglobin to lose its solubility and consequently aggregate and form fibers

Sickle-Cell Anemia is a Molecular Disease of Hemoglobin

51
Q

Explain transcription in eukaryotes

Explain the types of DNA editing

A

Transcription:
Prokaryotes: protein needed for transcription to take place-RNa polymerase holoenzyme
promoter region -nucleotide sequence in DNA that allows for particular proteins to bind to the DNA and start moving through the DNA and making RNa
RNa polymerase holoenzyme:it’s made up of core enzyme(consists of multiple sub units called two alpha proteins,two beta units,omega sub unit)this core enzyme reads DNA and makes RNa and the second constituent is the sigma sub unit or factor( this sub unit binds to the promoter region making core enzyme release away from the sigma sub unit and making it move down the DNA reading it from 3’ to 5’ and synthesize an RNa strand from 5’ to 3’ or it binds the polymerase to the promoter region causing it to be able to transcribe DNA)
When you make RNa in a prokaryotic cell from the RNa polymerase,it makes all the RNa in that prokaryotic cell.
Sigma sub unit is the transcription factor in prokaryotes.

Eukaryotic cells:
RNa polymerase I Enzyme :reads DNA and makes RNa.
It needs a protein to bind to the promoter region to let the RNa polymerase to bind to the DNA to read the DNA and make RNa . The protein is called general transcription factor.

General transcription factors are transcription factors used by RNa polymerase in eukaryotic cells

RNA polymerase I with transcription factors makes rRNA specifically.

  • [ ] RNA polymerase II and general transcription factors make mRNa specifically and SnRNAs
    Small nuclear RNAs (SnRNAs) are involved in splicing

RNA polymerase III and general transcription factors making tRNA specifically and a bit of SnRNA and a bit of rRNa but more of tRNA

RNA editing:
Types of DNA editing-
mRNa has already been formed
This mRNA has a nucleotide sequence that an enzyme can read and switch nucleotides with .
This sequence is called CAA .
This helps in making APo proteins specifically ApoB100 in hepatocytes

In enterocytes they have a special enzyme that modifies the same gene that makes ApoB100 to make a different protein.

The enzyme is called Cytidine Deaminase.
This deaminates the cytosine nitrogenous base and switches it with Uracil. Making UAA not CAA. This UAA is a stop codon so if you have the ribosome which will be reading and making a particular protein,when it gets to the point with UAA ,it’ll stop translation so the full protein isn’t formed. A smaller protein will be formed and this protein is called APo-B48.

So you take the same mRNA and modify it to produce a different protein. A completely different sized protein.

52
Q

Explain how to modulate the rate of transcription in eukaryotes
Explain the stages of transcription in both eukaryotes and prokaryotes
What does pre-mRNA undergoe to make it mature
How do SNRP cleave introns?
Explain alternate RNA splicing

A

How to
Modulate the rate of transcription in eukaryotes:
1.Enhancers -DNA sequences that increase transcription rate
Specific transcription factors bind to the enhancer region causing a looping of the DNA thereby bringing the enhancer region closer to the promoter region while general factors bind to the promoter region.
Now that the enhancer is closer to the promoter region. The specific transcription factor stimulates reading of DNA to make RNa
Enhancers can be either far upstream or far downstream usually but specific factors can bind to it to bring it closer to the promoter region
Steroid hormones and thyroid hormones synthesis are stimulated using this process by binding to the enhancer region or specific transcription factor
2. Silencers-decrease transcription rate
Same for silencers just that it binds to decrease reading of DNA.

Stages of transcription:
Initiation of transcription-
Differences in the initiation stage of transcription between prokaryotes and eukaryotes
Prokaryotes:promoter regions are called 1.negative 35 region( meaning from the start pint at which RNA polymerase starts reading DNA and making RNa if you go back 35 nucleotides that’s the point at which RNa poly will bind in prokaryotic cells. 2. Negative 10 region or pribnobox
3. +1 region or transcription start site (nucleotide at which you just read and start making the whole process of RNA)
Eukaryotes:promoter regions are called TATA box (thymine,adenine,thymine,adenine) which will be a particular recognition sequence within the promoter in eukaryotic cells or CAAT box or GC box. These boxes identify nucleotide areas at which the RNa polymerase type II and transcription factors will bind to.

Prokaryotes:
Polymerases is just one-RNa polymerase holoenzyme

Eukaryotes -RNa polymerase II and general transcription factors (example is transcription factors II D which contains a protein (TATA binding protein) that binds to the TATA box )

All these are needed for initiation to occur in each cell.

Step 2-Elongation (this step is the same in both eukaryotes and prokaryotes)
a.Template strand or antisense strand
b.Coding strand
When RNA polymerase read DNA,the strand they read is the template strand and they use the template strand to make the mRNa

RNA polymerase binds to the DNA through the initiation process and opens DNA and stabilizes the single stranded DNA molecule and it unwinds the DNA and reads the DNAfrom 3’ to 5’ and synthesizes RNA from 5’ to 3’
Proofreading function is not certain for RNA polymerase unlike in DNA replication

Easy way to understand is you unwind from 5’ to 3’ then still at 3’,you read what you’ve unwound from 3’ to 5’ then now at 5’ ,you synthesize rna from 5’ to 3’

In eukaryotes we can inhibit RNA polymerase using a toxin called Amanitin which is from mushrooms
Rifampicin inhibits RNA polymerase in prokaryotes

Termination:
Different in prokaryotes and eukaryotes
In prokaryotes there are two mechanism:
1. Rho-dependent termination -RNA polymerase reads DNA and makes RNA (any RNA). As it does this the Rho protein starts moving up the rna being synthesized,when it gets the RNA polymerase it pushes the RNA polymerase off the DNA or makes the polymerase break away from the DNA thus terminating the transcription process
2. Rho-independent termination-
Inverted repeats form within the DNA that the RNa polymerase is reading
RNa polymerase binds to the template strand ,reads the strand and makes RNa
As it starts doing so,it encounters an inverted repeat which is a sequence in the DNA .
The inverted repeat tends to want to interact with each other forming a hairpin loop full of the nucleotides that were repeated. The hairpin loop triggers the polymerase to hop off the DNA and terminate the transcription process
The loop causes enzymes to bind to the portion and cleave the RNA formed away from the rna polymerase

Eukaryotes:
As RNa polymerase makes rna it hits a nucleotide sequence where it reads and makes AAUAAA(a polyadenylation signal) on the RNA as it reads the DNA. This signal activates enzymes which come to the area where the sequence is and cleave the RNA from the RNA polymerase
So in the end there’s an mRNa with a polyadenyaktion signal on it .

  • [ ] Modification of RNA after transcription only occurs in eukaryotic cells:
    Heterogenous nuclear RNA or hnRNa which is an immature mRNa that goes through modifications to make mature mRNa

So after transcription the mRNa formed is immature so it undergoes post transcription modifications to become mature.

The modifications are:
On the 5’ end of the hnRNA there’s a triphosphate and an enzyme called RNA triphosphatase comes and cleaves off one of the phosphate groups leaving two phosphates on the end of the 5’ end.
Another enzyme called guanylyl transferase comes and adds GTP. When this happens two phosphates in the form of pyrophosphate are released and broken down by pyrophosphatase into individual phosphates ending up with a GMP(guanisinemonophosphate) molecule plus the two phosphates on the end of the 5’ end.
Another enzyme called methyl transferase adds a methyl group to the guanisinemonophosphate
This complex formed is called a 7-methylguanisine group or 5’ cap.
This whole process is called capping . This is used to help to initiate translation by serving as a signal sequence that allows it to interact with the ribosome to undergo translation. This also prevents degradation by nuclease enzymes that want to break down the RNa

Methyl transferase uses S adenysyl methionine (SAM) to add the methyl group. SAM Carries a methyl group and gives it to methyl transferase

On the 3’ end poly A polymerase has two arms . One arm has plenty Adenine nucleotides and identifies the polyadenylation signal on the 3’ end and then it takes the other arm and adds on all the adenine nucleotides to the polyadenylation signal which is AAUAAA. When this happens, it forms a tail on the 3’ end with plenty adenine nucleotides. This tail is called polyA tail (this tail is used to initiate translation process and helps to decrease degradation by nuclease . Also help transport hnRNA out of the nucleus into the cytosol. )

Splicing : this occurs after the Capping and formation of poly A tail occur
In the hnRNA. In the hnRNA there are specific nucleotides that will be read, translated and will code for particular amino acids.these nucleotides are called Exons.
There are other nucleotides that will not be read and do not code for any amino acid. These are called Introns.
Splicing is getting rid of Introns or intervening sequences and stitching together the Exons.
Molecules are needed for splicing to occur
Molecules such as Small nuclear RNA
And SnRNA combine with proteins to make a SNRP.(small nuclear ribonuclear proteins). SNRP bind to hnRNA and cleave the introns and stitch together the exons.
Thus forming mRNA finally.

In the mRNA now produced,we have a 5’ cap,the exons and the poly-A tail.
Between the 5’ cap and the exons is a region called the 5’ untranslated region and the region between the exons and the poly-A tail is called 3’ untranslated region.

How do SNRP cleave introns?
5’Exon1 3’(nucleotide sequence here which is GU )Intron1(nucleotide sequence here which is AG)5’Exon2 3’
They bind near the intron. There’s a specific nucleotide sequence between the 3’ splice site near exon 1 and the beginning of intron 1 and another specific nucleotide sequence near the 5’ splice site near exon 2 and at the end of intron 1.
The nucleotide sequence is GU(I’m a G wbu),AG(am a G)
There’s another nucleotide (which is Adenine)at the branch point or in the middle of the intron and the Aadenine has a specific OH group .
The SNRP cleave at the 3’ splice site (with an OH cuz OH is on 3’ end) near exon 1

The OH group at the Adenine binds or attacks the GU site and pulls it making it attach to the Adenine thereby creating a loop.
The 3’ OH on exon 1 then sees the the 5’ splice site near Exon 2 and attacks it.
This makes the nucleotide sequence AG break away from exon 2.
Leaving Exon 1 fused with Exon 2,spitting out The intron.

Spinal muscular atrophy(affects anterior gray horn neurons making them develop lower motor neuron lesions) :there’s a deficiency in SMN protein because the SNRP isn’t working properly so plsicing doesn’t occur well

Beta thalassemia- there’s a particular intron that isn’t removed causing a protein to be made that isn’t normal thereby producing beta thalassemia.

Alternative RNA splicing:
It gives variants of a protein
SNRP splices leaving introns behind and three diff mRNA strands being formed . One strand making a protein called protein A
Second strand popping out introns and Exon 2. Leaving behind Exon 1 and Exon 3. This gives an MRNa that will code for another protein called protein B

Third strand popping out introns and cutting out Exon 3. Leaving behind Exon 1 and exon 2. Giving an mRNa that will code for another protein called protein C

This makes a protein from tHe same gene but variants of that protein.
Example in plasma cells that make antibodies,we have antibodies that can be secreted or we can have antibodies that will be expressed on the cell membrane.
Differences in antibodies,dopamine receptors of the brain are examples of alternate RNA splicing

53
Q

UCC:
What are the advantages of the double helix bond?
Look at the types of DNA from legon slide
A=T,G=C but AT=GC
Generally GC~50% but extremely variable . Example G-C content for Slime mold is ~22% and mycobacterium is ~73%
What’s the important of G-C content?
What is G-C content
How is it measured

Why are there so many deviations from normal conformation in DNa ?

A

Stability- it protects bases from attack by water soluble compounds and water itself
It provides easy mechanisms for replication

In polymerase chain reaction (PCR) experiments, the GC-content of short oligonucleotides known as primers is often used to predict their annealing temperature to the template DNA. A higher GC-content level indicates a relatively higher melting temperature

increased GC content and an increased level of transcription

GC-content (or guanine-cytosine content) is the percentage of nitrogenous bases in a DNA or RNA molecule that are either guanine (G) or cytosine (C).[

DNA with low GC-content is less stable than DNA with high GC-content; however, the hydrogen bonds themselves do not have a particularly significant impact on molecular stability, which is instead caused mainly by molecular interactions of base stacking.

measure the melting temperature of the DNA double helix using spectrophotometry.

GC is slightly denser
Higher GC DNa moves further in a gradient
Higher number of base pairs = more stable DNa that is the strands don’t separate as easily

Remember that G-C has three hydrogen bonds between it while A-T or A-U has two hydrogen bond

Because it has effects on transcription or gene expression ,it may also serve in packaging and it enhances responsiveness that’s why there are many deviations
Note: most cellular DNa exists as a protein containing super coils

54
Q

UCC:
What is DNa denaturation
What is DNa replication and what is it’s biological significance
When does replication occur in eukaryotes
State the rules of replication
State the 3 possible models of DNa replication and explain them
What experiment demonstrated that DNa is replicated in a semi conservative manner. Explain this experiment

A

When a DNA solution is heated enough, the double-stranded DNA unwinds and the hydrogen bonds that hold the two strands together weaken and finally break. The process of breaking double-stranded DNA into single strands is known as DNA denaturation, or DNA denaturing.

Replication is the process id duplication of the entire genome prior to cell division

Significance:extreme accuracy of DNA replication is necessary in order to preserve the integrity of the genome in successive generations

It occurs in the S phase of the cell cycle
Replication rate I. Eukaryotes is slower resulting in a higher fidelity or accuracy of replication in eukaryotes

Rules:
Semi conservative
Starts at the ‘origin’
Synthesis always in the 5’ to 3’ direction(remember it unwinds from 5’ to 3’,is read from 3’ to 5’ and is synthesized from 5’ to 3’)
Can be uni or bidirectional
Is semi discontinuous(check the legon own for the definition of this)
RNA primers are required

Models:

a. Semi conservative
b. conservative
c. dispersive

Semi-conservative replication. In this model, the two strands of DNA unwind from each other, and each acts as a template for synthesis of a new, complementary strand. This results in two DNA molecules with one original strand and one new strand. Or one strand of duplex passes on unchanged to each of the daughter cells. This conserved strand acts as a template for the synthesis of a new complementary strand by the enzyme DNA polymerase (take note of the spelling. It’s complementary not complimentary)
The original double helix strands separate and the complementary bases align opposite templates. Enzymes link sugar phosphate elements of aligned nucleotides into a continuous new strand
Conservative replication. In this model, DNA replication results in one molecule that consists of both original DNA strands (identical to the original DNA molecule) and another molecule that consists of two new strands (with exactly the same sequences as the original molecule).
Dispersive replication. In the dispersive model, DNA replication results in two DNA molecules that are mixtures, or “hybrids,” of parental and daughter DNA. In this model, each individual strand is a patchwork of original and new DNA.

Meselson-Stahl experiment.
Control group: E. coli grown for many generations in superscript 14 N medium. Extract DNA from cells,centrifuge
1. E. coli grown for many generations in superscript 15 N medium.
Extract DNA from cells
Centrifuge . DNa bands in cesium chloride gradient
2. Superscript 15 N cells transferred to superscript 14 N medium. Cells replicate once to produce first generation of daughter cells. Extract DNA from cells ,centrifuge,put DNA bands in cesium chloride gradient with the Superscript 14 N and 15 N

After thirty minutes,
3. Cells replicate a second time tk rosicue a second generation of daughter cells. Extract DNA from cells. Centrifuge . And now the gradient will contain Superscript 14 N and 15 N from the control group Superscript 14 N

55
Q

Explain the rule DNa starts at the origin and it is uni or bidirectional
Where is the energy gotten for DNa replication
Explain DNA replication is semi discontinuous and RNa primers required (check from the notes from legon)

A

Initiator proteins identify specific base sequences on the DNA called the sites kf origin
In prokaryotes it’s just one single origin site example in E coli it’s oriC
But in eukaryotes it’s multiple sites of oigin(replicator). Example yeast it’s ARS(autonomously replicating sequences)

Uni or bidirectional: replication forks more in one or opposite directions

In bidirectional synthesis, the replication process occurs in two directions. In unidirectional replication only one replication fork is formed. In unidirectional replication, only one end of the replication eye is moving or growing. In bidirectional replication, both the ends are moving.

DNA replication is bidirectional and discontinuous; explain your understanding of those concepts. At an origin of replication, two replication forks are formed that are extended in two directions. On the lagging strand, Okazaki fragments are formed in a discontinuous manner.

Bidirectional replication involves replicating DNA in two directions at the same time resulting in a leading strand (were replication occurs more rapidly) and a lagging strand (with slower replication).

People also ask
How DNA replication is bidirectional and discontinuous?

DNA replication is bidirectional and discontinuous; explain your understanding of those concepts. At an origin of replication, two replication forks are formed that are extended in two directions. On the lagging strand, Okazaki fragments are formed in a discontinuous manner.
https://opentextbc.ca › chapter › d…
DNA Replication in Prokaryotes – Biology 2e - BC Open Textbooks
More results
What is DNA replication unidirectional?
In unidirectional replication, growth proceeds along both strands in the same direction leading from the origin. Along one of the parental template strands, synthesis of the new complementary strand takes place by the continuous addition of nucleotides to the available 3′ end of the forming strand.

This energy comes from the nucleotides themselves, which have three phosphates attached to them (much like the energy-carrying molecule ATP). When the bond between phosphates is broken, the energy released is used to form a bond between the incoming nucleotide and the growing chain.

Semi discontinuous: meaning anti parallel strands are replicated simultaneously
Leading strand synthesis continuously in 5’ to 3’
Lagging strand synthesis in fragments in 5’ to 3’
New strand synthesis always in the 5’ to 3’ direction

56
Q

State the core Proteins at the replication fork

A

Topoisomerases-prevent torsion by DNa breaks
Helicase-separates 2 strands
Primase -RNa primer synthesis
Single strand binding proteins: prevents reannealing of single strands
DNA polymerase - synthesis of new strand
Tethering protein-stabilizes polymerase
DNa ligase -seals nick via phosphodiester linkage

57
Q

UCc-
Trial questions
Which bases are purines,which are pyrimidines?
If a purine were substituted for a pyrimidine at a single position in one strand of a DNA double helix what would happen?
In a DNA double helix why doesn’t an A or T form two hydrogen bonds (out of the three possibles) with G or C?
How many kinds of 5 memebered rings are in DNA?
How many kinds of 6 memebered rings are in DNA?
Does the free arm of deoxyribose (the carbon that is not a member of the pentose ring) point in the direction in which the coding strand is read or against it?
Eukaryotic chromosomes have multiple origins of replication true or false?
In what direction is the newly synthesized DNA produced?
1. 5’ -3’
2. 3’-5’
3. In the direction of the major groove
4. Both 5’-3’ and 3’-5’ depending on which strand is being replicated

Nucleotides are always added to the growing DNA strand at the 3’ end at which the DNA has a free _____ on the 3’ carbon of its terminal deoxyribose.

  1. Phosphate group
  2. Hydroxyl group
  3. Nitrogen base
  4. Methyl group

The E. coli chromosome has 4.7x10 raised to the power 6 bp; a bidirectional replication fork progresses at about 1000 nucleotides per sec. Therefore the minimum time required to complete replication is?

  1. 12 min
  2. 24 min
  3. 39 min
  4. 78 min
  5. 120 min
What is the sequence (1 to 6)  in which these proteins function during DNA replication?
\_\_\_\_\_RNA primase
\_\_\_\_\_DNa ligase
\_\_\_\_\_DNa polymerase 
\_\_\_\_\_Topoisomerase 
\_\_\_\_\_DNa Helicase 
\_\_\_\_\_tethering proteins

Why is an RNA primer necessary for DNA replication?
A. The RNA primer is necessary for the activity of DNA ligase
B. The RNA primer creates the 5’ and 3’ ends of the strand
C. DNA polymerase can only add nucleotides to RNA molecules
D. DNA polymerase can only add nucleotides to an existing strand

A

Answers:

58
Q

UCc-State the differences between bacterial,animal and plant cells
Find the diseases a problem with each organelle causes

A

Exterior structure:
Cell wall- present in bacterium(protein polysaccharide),absent in animals,present in plants(cellulose)

Plasma membrane- present in all three

Flagella (cilia)- sometimes present in both bacterium and animal cells but in plant cells the sperm of a few species posses flagella

Interior structures and organelles:
Endoplasmic reticulum- absent in bacterium,usually present in both animal and plant

Microtubules-absent in bacterium,present in both animal and plant

Centrioles: absent in both bacterium and plant cell. Present in animal cell

Golgi apparatus: absent in bacterium,present in the other two cells

Nucleus: absent in bacterium present in the other two

Mitochondria: absent in bacterium,present in other two

Chloroplast: absent in bacterium and animal but present in plant

Chromosomes: a single circle of naked DNA in bacterium ,multiple units ,DNA associated with protein for both animals jd plant cells

Ribosomes: present in all three
Lysosomes: absent in bacterium,present in other two

Vacuoles: absent in bacterium,absent or small in animal,usually a large single vacuole in mature cell for plant