Biological molecules Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

How do polar molecules lead to the formation of hydrogen bonds

A
  • Polar molecules = covalent molecules in substances causing an unequal share of electrons amongst the molecules hence creating regions of positivity and negativity, for example in oxygen and hydrogen there is always a larger share of electrons in oxygen - hence all hydroxyl groups including water are polar
  • Polar molecules interact with each other as slightly positive region attracts slightly negative regions - this forms hydrogen bonds (which are weak)
  • Hydrogen bondings weak but high number of bonds gives water its special characteristics
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

List and explain the key characteristics of water

A
  • Unusually high boiling point - water is lighter than gases (e.g. carbon dioxide, oxygen) but still it is a liquid in room temp and has a high boiling point - because of hydrogen bonding between molecules
  • Ice floats - Usually substances = more dense when solid then liquid but this is the opposite for water - Happens because of how hydrogen bonds fix positions of the polar molecule further apart than in liquid state. This produces a giant rigid but open tetrahedral structure of hydrogen atoms making it less dense solid then liquid.
  • Cohesive - Water moves as one mass because mols are attracted to each other (cohesion) -
  • Adhesive - Water mols are attracted to other materials too which is adhesion
  • Surface tension - water = more cohesive than adhesive to air causing water to have a skin of surface tension
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How does water aid life - give 6 examples

A
  • Solvent - acts as solvent in which many solutes in an org can be dissolved - cytosol of prokaryotes & eukaryotes = mainly water. Many solutes inc. polar mols, amino acids, proteins, nucleic acids. This allows water to act as a medium for chemical reactions and helps transport dissolved substances in and out of cells.
  • Transport medium - Cohesion allows mols to stick together in water. Adhesion and cohesion work together to exhibit capillary action which allows water to rise up against gravity
  • Coolant - Helps buffer temps during chemical rxns in eukaryotic and prokaryotic because of the large amounts of energy needed to break the many hydrogen bonds in water. Maintenance of constant temp = important - to allow enzymes to work
  • Constant environment - Allows fishes and animals at sea to live in water
  • Ice floats - Gives insulating layer to water below which keeps temp constant and survivable allowing aquatic animals to move around, live and not be frozen
  • Surface tension - Strong enough to support some animals who inhabit surface water - pond skaters
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Which chemical elements make up: Carbohydrates, lipids, proteins and nucleic acids

A
  • C, H and O for Carbohydrates
  • C, H and O for lipids
  • C, H, O, N and S for proteins
  • C, H, O, N and P for nucleic acids
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Describe the structure and differences between pentose monosaccharide and hexose monosaccharide (including alpha-glucose and beta glucose)

A

Pentose monosaccharide = ribose

  • It has 5 carbon atoms
  • Lacks a carbon atom and a hydroxyl group + H on this 1 carbon compared to Hexose monosaccharide
Hexose monosaccharide = Glucose
- 6 Carbon atoms 
- 2 types:
alpha-glucose & Beta-glucose, 
The difference is that on carbon 1 the hydroxyl group is on opposite positions (in alpha the hydroxyl group is at the bottom, in beta it`s at the top)

See diagrams in folder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

How are disaccharides sucrose, lactose and maltose formed from glycosidic bonds

A
  • Dissacharides form when two monosaccharides join together by glycosidic bond
  • This is a condensation reaction
  • The reaction is reversible thus it can be reversed by a synthesis reaction of hydrolysis
  • Maltose is formed as two alpha glucose molecules form a glycosidic between carbon 1 - this is a 1,4 glycosidic bond
  • Sucrose is formed when glucose and fructose form glycosidic bonds together
  • Lactose is formed when glucose combines with galactose
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Describe and explain the structure of starch and how it`s properties relate to their functions in living organisms

A
  • Made up of many bonds joined together by glycosidic bonds to form two different polysaccharides (amylose and amylopectin) which combine to create starch
  • Starch is used as an energy store in plants - Release glucose for respiration - hydrolysis reaction - enzymes act as catalysts

Amylose

  • formed by alpha 1,4 glycosidic bonds
  • Angle of chains creates a helix which is stabilised by hydrogen bonds
  • The stabilised helix makes amylose more compact and less soluble then glucose
  • see diagrams in mindmap

Amylopectin

  • all formed by alpha glucose
  • mostly formed by 1,4 glycosidic bond, some 1,6 glycosidic bond
  • 1,6 glycosidic bonds allow for branching which creates more access points for quicker energy release
  • see diagrams in mindmap
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Describe and explain the structure of glycogen and how it`s properties relate to their functions in living organisms

A
  • Chemical energy store in Animals and fungi
  • Release glucose for respiration = hydrolysis reaction
  • All formed by alpha glucose
  • Mostly formed by 1,4 glycosidic bond, some 1,6 glycosidic bond but more then amylopectin
  • 1,6 glycosidic bonds make it more compact thus storing more energy that animals need as they more active then plants, also allows for more access points for enzymes to add or remove glucose - speeds up process - increases respiration
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe and explain the structure of cellulose and how it`s properties relate to their functions in living organisms

A
  • Used to form cell walls in plants, Essential for healthy digestive system as it forms necessary fibre and roughage of digestive system
  • Made up of b-glucose (beta glucose) formed together by 1,4 glycosidic bonds.

Beta-Glucose bonds

  • B-glucose molecules are not easily joined together because the hydroxyl groups on carbon 1 and 4 are too far apart to reach
  • To counter this, alternate b-glucose molecules invert 180 degrees 0 this allows them to join and means that there are no coils or branches - just straight chains of cellulose
  • Thus straight chains of cellulose are produced parallel to each other, this results in the hydroxyl groups being very close which leads to the formation of hydrogen bonds between adjacent hydroxyl groups
  • Collection of thousands of hydrogen bonds = cellulose - V. Strong
  • The cross-links of hydrogen bonds result in chains becoming stronger fibres
  • First they bond together to form microfibrils - these join together to form microfibrilis
  • These combine to form V. strong cellulose fibres
  • Diagrams on mind map
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Describe and explain the structure of a triglyceride

A
  • A triglyceride is made by combining 1 glycerol molecule (alcohol) with 3 fatty acids (carboxylic acids)
  • Both molecules contain hydroxyl group which bond together to form ester bonds in a process called esterification (example of a condensation rxn)
  • 3 Water molecules are relased as a by-product
  • Diagram in folder
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are Saturated and Unsaturated fatty acids and why are they significant

A
  • Fatty acids with no double bonds between carbon atoms = saturated
  • Fatty acids with carbon double bonds = unsaturated - two or more double bonds = polysaturated
    one double bond - monosaturated
  • Presence of double bonds causes molecules to kink/bend - thus they cannot pack together as closely and remain liquid at room temp - described as oils rather than fats
  • Plants contain unsaturated triglycerides as oils (usually)
  • An excess in saturated fat can lead to coronary heart disease
  • Excess of any type of fats leads to obesity leading to a strain on the heart
  • For diagrams check folder
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Describe and explain the structure of phospholipids

A
  • Contain phosphorous, Carbon, Hydrogen and Oxygen
  • Inorganic phosphates ions found in cytoplasm
  • Phosphate ions = extra electrons = soluble in water
  • To make a phospholipid one fatty acid chain = replaced with a phosphate group
  • So there are - two fatty acids, glycerol and a phosphate group
  • The phosphate group is charged, making the head of the phospholipid hydrophilic but the fatty acid tail of a phospholipid is not charged and hydrophobic
  • This dual hydrophobic/hydrophilic structure forms a layer on the surface of the water with it`s phosphate head in the water but the fatty acid tail sticking out of the water = surfactant/ surface active agents
  • Can also form structures based on a bilayer - all hydrophilic tails point towards centre of the sheet and hence are kept away from the water.
  • This allows them to separate an aqueous environment from the aqueous cytosol within cells - thus phospholipids play a key role in forming cell membranes for cells or organelles
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Describe and explain the structure, properties and function of sterols (cholestrol in particular)

A
  • Type of lipid, AKA steroid alcohols
  • Complex alcohol mols with a four carbon ring structure and hydroxyl group at the end
  • Have dual hydrophobic/hydrophilic characteristics
  • Hydroxyl groups = polar = hydrophilic
  • Rest of molecules = hydrophobic

Cholestrol

  • Cholesterol = sterol
  • Manufactured in liver and intestines
  • Important role in cell membranes - add stability and regulates fluidity - It does so by strategically positioning in between phospholipids. - keeps membrane fluid in low temp and stops it from becoming too fluid at high temp
  • Vitamin D, Steroid hormones & bile made using cholesterol
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Role of lipids in the body

A

Due to being non-polar lipids have roles in:

  • Membrane formation & creation of hydrophobic barriers
  • Hormone production
  • Electrical insulation - important for impulse transmission
  • Waterproofing - bird`s feather, plant leaves
  • Lipids esp. triglycerides - important role in long-term energy storage - under skin around vital organs where they provide - thermal insulation, cushioning to protect organs, Buoyancy for aquatic animals e.g. whales
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the general structure of amino acids and what are essential amino acids

A

R
-
(amine group) H2N —— C ——- COOH (carboxyl group)
-
H

  • 20 different amino acids
  • Different R group = different amino acid
  • ## Essential amino acids are amino acids that have been taken in through diet because they cannot be created or converted in the body
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Synthesis and breakage of polypeptides and dipeptides

A
  • Amino acids join together by forming peptide bonds with a condensation reaction
    This happens by:
  • the amine and carboxylic acid groups connected to the central carbon atom react
  • The hydroxyl in the carboxylic group reacts with a hydrogen in the amine group of the other amino acid
  • A peptide bond is formed between the amino acids and water is released
  • The resulting compound is a dipeptide
  • When more then two amino acids are joined together a polypeptide is formed - reaction is catalysed by the enzyme - peptidyl transferase
  • To break a peptide bond, a hydrolysis reaction takes place - proteases (enzyme) catalyse this reaction
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Describe and explain the primary protein structure

A
  • Sequence of chain of amino acids as directed by info carried in DNA
  • Bonds involved = peptide bonds
  • Particular amino acids in sequence influence how the polypeptide folds - this will go on to determine the function of the protein
18
Q

Describe and explain the secondary protein structure

A
  • Oxygen, Hydrogen and Nitrogen atoms of the basic repeating structure of amino acids interact (r-groups still not involved)
  • At this point the polypeptide chain is not straight, it is either a alpha-helix or a beta pleated sheet
  • Hydrogen bonds involved at this point

Alpha helix
- The shape for this chain is a helix

Beta Pleated sheet

  • The shape is those of pleated sheets
  • Here the polypeptide chains lie parallel to one another and are joined by hydrogen atoms
19
Q

Describe and explain the tertiary protein structure

A
  • Here the protein folds into it`s final shape
  • The coiling or folding of sections of proteins in the secondary protein structure lead the different r-groups to be close enough to react together
  • Produces precise & unique shapes for specific functions

The following interactions then occur between the r-groups:

  • Hydrophobic and hydrophilic interactions - weak interactions between polar and non-polar r-groups
  • Hydrogen bonds - weakest bonds
  • Ionic bonds - Stronger than hydrogen bonds - forms between oppositely charged r-groups
  • Disulfide bridges - Covalent and the strongest bonds - only form between r-groups containing sulfur atoms
20
Q

Describe and explain the Quartenary protein structure (examples are not necessary yet)

A
  • Two or more individual proteins (called subunits) associate together
  • The protein subunits could be identical or different

The following interaction then occur between the different proteins:

  • Hydrophobic and hydrophilic interactions - weak interactions between polar and non-polar r-groups
  • Hydrogen bonds - weakest bonds
  • Ionic bonds - Stronger than hydrogen bonds - forms between oppositely charged r-groups
  • Disulfide bridges - Covalent and the strongest bonds - only form between r-groups containing sulfur atoms

Examples:

  • Enzymes often consist of two identical sub-units
  • Insulin (hormone) has two different subunits
  • Haemoglobin has four subunits made up of two sets of two identical subunits`
21
Q

Describe and explain the general structure and function of globular proteins and cite Insulin as an example

A
  • Compact, water soluble and roughly spherical in shape
  • Form when proteins fold in such a way that the hydrophobic r-groups on the amino acids are kept away from the aqueous environment whilst the hydrophilic r-groups are on the outside of the protein - allows globular protein to be soluble
  • Solubility = v important for the different functions of globular proteins - essential for regulating many of the processes necessary to life

Insulin

  • Good example of a globular protein necessary in the body
  • Hormone involved in regulating blood concentration - needs to be transported in the blood - so solubility is V important
  • Insulin (as a hormone) needs to fit into specific receptors on cell-surface membranes to have an effect - therefore they need precise shapes
22
Q

Describe and explain the general structure and function of conjugated proteins and cite Haemoglobin and Catalase as an example

A
  • These are globular proteins that contain a non-protein group called a prosthetic group
  • Proteins without prosthetics = simple proteins
  • Lipid or Carbs can combine to form - lipoprotiens or glycoproteins
  • Metal ions and molecules derived from vitamins also form prosthetic groups
  • Haem groups are examples of prosthetic groups - contain an iron (Fe2+)

Haemoglobin

  • Red oxygen carrying pigment in red blood cells
  • Quaternary protein made from polypeptides (two alpha subunits and two beta subunits)
  • Each subunit contains a prosthetic haem group
  • The iron ions present in the haem groups are able to reversibly combine with an oxygen molecule allowing haemoglobin to transport lose and gain oxygen molecules when and where needed

Catalase

  • Catalase is an enzyme - therefore it needs a very specific shape
  • Quaternary protein contains 4 prosthetic haem groups
  • The presence of Iron II ions in the prosthetic groups allows catalase to interact with hydrogen peroxide and speed up it`s breakdown - hydrogen peroxide = common byproduct of metabolism which ca be harmful if allowed to accumulate
23
Q

Describe and explain the properties and functions of Fibrous proteins and Keratin, Elastin and Collagen as examples

A
  • Formed from long, insoluble molecules - result of a high proportion of hydrophobic amino acid r-groups in the primary structure
  • Limited range of amino acids with usually small r-groups
  • Amino acid sequence in primary structure = usually repetitive
  • Leads to very organised structures reflected in the roles fibrous proteins have
  • Tend to make strong long molecules which are not folded into complex 3-d shapes like globular

Keratin

  • Group of fibrous protein in hair, skin and nails
  • Large proportion of Cysteine (sulfur-containing amino-acid) - Many strong disulfide bridge - makes it strong, inflexible, insoluble
    Amount of disulfide bonds/bridges determines flexibility - e.g. hair has less disulfide bonds = less flexible, nail has more disulfide bonds = more flexible
  • Unpleasant smell from burning hair skin or nails = sulfur burning

Elastin

  • Found in elastic fibres - present in walls of blood vessels and alveoli - give structures necessary flexibility to expand but also recoil
  • Quaternary proteins made from stretchy molecules = tropoelsatin

Collagen

  • Connective tissue found in skin, tendons, ligaments, nervous system
  • Different forms but all made of three polypeptides wound together in a long rope-like structure
  • Collagen has necessary flexibility
24
Q

List the key inorganic ions involved in biological processes

A

Cations:

  • Calcium ions(Ca2+)
  • Sodium ions (Na+)
  • Potassium ions (K+)
  • Hydrogen ions (H+)
  • Ammonium ions (NH4+)

Anions:

  • Nitrate (NO3-)
  • Hydrogencarbonate (HCO3-)
  • Chloride (Cl-)
  • Phosphate (PO43-)
  • Hydroxide (OH-)
25
Q

PAGs

A

PAG 9, PAG 5, PAG 6

26
Q

Describe and explain the structure of nucleotides as monomers forming nucleic acids in both RNA and DNA

A
  • Contain the elements Carbon, Hydrogen, Oxygen, Nitrogen and Phosphorous
  • Nucleic acids are large polymers formed from nucleotide monomers linked in a chain

Individual nucleotide is made of three components:

  1. ) Pentose monosaccharide (sugar containing five carbon atoms) - Deoxyribose in DNA, Ribose in RNA
  2. ) A Phosphate group (PO42-) - inorganic and acidic
  3. ) Nitrogenous base - Complex organic molecule containing one or two carbon rings in its structures as well as Nitrogen - this is where pyrimidines (Thymine, Cytosine - thymine is replaced for uracil in RNA) or purines (Adenine, Guanine) are
27
Q

Synthesis and breakdown of polynucleotides

A
  • Nucleotides are linked together by condensation reactions to form a polymer called polynucleotides
  • The phosphate group of one nucleotide at the fifth carbon of the pentose sugar forms a covalent phosphodiester bond with the hydroxyl group of the phosphate at the third carbon of the adjacent nucleotide
  • This forms a strong sugar-phosphate backbone with a base attached to each sugar
  • Phosphodiester bonds are broken by hydrolysis reactions - releasing individual nucleotides
28
Q

Describe and explain the structure of DNA

A
  • Deoxyribonucleic Acid
  • Sugar in DNA nucleotides = deoxyribose - one fewer oxygen atom then ribose
  • Varies in length from a few nucleotides to millions
  • Made up of two strands of Polynucleotides coiled into a double helix
  • The double helix is held together by hydrogen bonds between the bases like the rungs of a ladder.
  • Each strand has a phosphate group (5’) at one end and a hydroxyl group (3’) at the other end
  • The two parallel strands are arranged into an anti parallel structure (arranged so that the parallel strands they run in opposite directions)
  • Four different bases in DNA - Pyrimidines - Thymine, Cytosine - Purines - Guanine, Adenine
  • Adenine and Thymine - able to form two hydrogen bonds together - so can only bind with each other
  • Guanine and Cytosine - able to form three hydrogen bonds together - so can only bind with each other
  • Complementary base pairing
  • Thus by a small pyrimidine base always binding with a larger purine base means that it can maintain a constant distance between the DNA backbones, resulting in parallel polynucleotide chains
  • Due to complementary base pairing DNA always has the same number of bases
29
Q

Describe and explain how DNA replication takes place in 4 steps

A

The process in 4 steps:

  1. ) DNA helicase (an enzyme causes) the two strands of the DNA to separate as it catalyses reactions leading to the breakage of hydrogen bonds between the different bases
  2. ) As the two strands are separated free nucleotides in the nucleus attach to their complementary bases,
  3. ) Once the free nucleotides have lined up to their complementary base pairs - they are joined together by DNA polymerase
  4. ) Finally, all the nucleotides are joined to form a complete polynucleotide chain using DNA polymerase - thus two identical molecules of DNA are formed - each new one will have one original strand meaning the new molecule of DNA is semi-conservative and the process is known as - “Semi-conservative replication”
  • Sometimes sequences of bases are not matched exactly - an incorrect sequence may occur in the new strand- these errors are random and spontaneous - known as mutations
30
Q

Why is DNA replication important?

A
  • DNA replication is important in copying DNA for genetically identical daughter cells produced as a result of cell division which is key in growth and replacing dead cells
31
Q

What is meant by the genetic code being in triplets?

A
  • This refers to the idea that DNA carries instructions in a sequence of bases which is a simple triplet code known as a codon
32
Q

How is DNA non-overlapping?

A
  • The bases in the genetic code do not overlap but are in sequences - this is ensured by having a codon that starts the sequence allowing codons to be read “in frame” - thus given it`s in triplets and has start and end codons it is non-overlapping
33
Q

How is DNA degenerate?

A
  • Many amino acids can be coded for by more than one codon because there are more combinations of codons possible then there are amino acids
  • Therefore DNA is degenerate
  • Refer to the DNA code wheel to see which codons code for different amino acids
34
Q

How is DNA universal?

A
  • Because all organisms use the same code but the sequences coding for each individual protein will be different
35
Q

Outline how transcription takes place in 5 steps

A
  1. ) The section of DNA containing the gene unwinds and unzips under the control of DNA helicase (catalyses the breakage of hydrogen bonds between bases) beginning at the start codon
  2. ) Then using the antisense strand (3’ to 5’) (this strand does not code for the protein) as a template strand the RNA strand forms carrying the same base sequence as the sense strand (needed to code for the protein)
  3. ) This happens as free RNA nucleotides will base pair with complementary bases exposed on the anti-sense strand. (thymine is replaced for uracil)
  4. ) Phosphodiester bonds are formed between the RNA nucleotides by the enzyme RNA polymerase. Transcription stops at the end of the gene forming the completed mRNA
  5. ) mRNA detaches from DNA template and leaves the nucleus through the nucleus pore.
36
Q

Outline how translation takes place in 6 steps

A
  1. ) The mRNA binds to the small subunit of the ribosome at it`s start codon
  2. ) A tRNA with the complementary anticodon binds to the mRNA start codon. This tRNA carries the corresponding amino-acid
  3. ) Another tRNA with the complementary anticodon binds to the next mRNA codon and carries the corresponding amino-acid. Only a maximum of two RNAs can be bound at the same time
  4. ) The first amino acid is then transferred to the amino acid on the second tRNA by the formation of a peptide bond - this is catalysed by the enzyme peptidyl transferase - an rRNA component of the ribosome
  5. ) The ribosome then moves along the mRNA and releases the first tRNA making the second tRNA become the first
  6. ) Steps 3-5 are repeated until the ribosome reaches the end of the mRNA at a stop codon and the polypeptide is released
37
Q

Describe and explain how the polypeptide released from translation forms into a protein

A
  • Amino acids have been joined together by the mRNA and so the primary structure of the protein has been formed
  • They then fold into secondary and tertiary structures as dictated by the sequence of amino acids in the primary structure
  • The protein may undergo further modification in the golgi apparatus
38
Q

What is the role of rRNA in translation and protein synthesis in general

A
  • rRNA = ribosomal RNA
  • Ribosomes are composed of two subunit RNAs - one small, one large
  • Important in maintaining structural stability of protein synthesis sequence and plays a biochemical role in catalysing the reaction
39
Q

What is the role of tRNA in translation and protein synthesis in general

A
  • tRNA = transfer RNA
  • Composed of a strand of RNA folded in such a way that three bases are at one end of the molecule - this is the anti-codon
40
Q

Note the basic structure of ADP and ATP

A
  • Comprises a pentose sugar (ribose), a nitrogenous base (adenine) and inorganic phosphates
41
Q

Describe the functions of glycoproteins in the cell surface membrane

A
  • Acting as receptors for cytokines; hormones by acting as binding sites
  • Cell signalling, cytokines, transport proteins
  • Cell recognition, act as antigens showing the cell to be self or non-self
  • Stability - for plasma membrane by binding with water molecules, adhesion between cells and tissues