Biological Molecules Flashcards

1
Q

What are the functions of water?

A
  • Water is a reactant (part of many reactions e.g. hydrolysis)
  • Water is a solvent (many substances dissolve in it e.g. ions in water into the blood and many biological reactions take place in a solution)
  • Water transports (substances e.g. glucose, mineral ions, oxygen gas)
  • Water is involved in temperature control (has high specific heat capacity and high latent heat of evaporation)
  • Water is a habitat (contains oxygen and nutrients can be dissolved in it and it doesn’t change temperature rapidly as the H bonds absorb a lot of energy)
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2
Q

How does hydrogen bonding occur between water molecules?

A

A molecule of water is one atom of O joined by 2 atoms of H by shared electrons. So, the shared negative H electrons are pulled towards the O atom, the other side of each hydrogen atom is left with a slight positive charge. The unshared negative electrons on the O atom give is a slight negative charge. Making water a polar molecule. The slightly negative and positively charged atoms of other water molecules interact with each other causing attraction which is called hydrogen bonding.

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3
Q

How is water less dense as a solid than a liquid?

A

Water molecules are held further apart in ice than they are in liquid water because each water molecule forms 4 hydrogen bonds to other water molecules, making a lattice shape. This makes ice less dense than water. This is also why ice floats.

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4
Q

What is the Biomolecule name for:
- Carbohydrates
- Lipids
- Proteins
- Nucleic acids

A
  • Carbohydrates = C, H, O
  • Lipids = C, H, O
  • Proteins = C, H, O, N, S
  • Nucleic acids = C, H, O, N, P
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5
Q

What is a condensation reaction?

A

A reaction in which two molecules join together by a chemical bond with the release of a water molecule. E.g. when two glucose molecules bond together.

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6
Q

What is a hydrolysis reaction?

A

Hydrolysis is the opposite of a condensation reaction and is when water is added to break a chemical bond between two molecules.

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7
Q

Name of bonds in carbohydrates:

A

Glycosidic bonds

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8
Q

What are the two forms (isomers) of glucose and how are they different?

A

The two isomers of the monosaccharide are a-glucose (alpha) and b-glucose (beta). In a-glucose both hydroxyl groups are below their respective H groups. In b-glucose one hydroxyl group is above the H group and one stays below.

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9
Q

Examples of disaccharides and how they are formed:

A
  • Maltose is formed by condensation of two glucose molecules
  • Sucrose is formed by condensation of glucose and fructose
  • Lactose is formed by condensation of glucose and galactose
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10
Q

What are polysaccharides?

A

They are macromolecules consisting of more than 2 sugars - often a long chain polymer - joined by glycosidic bonds. They are not sugars.

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11
Q

Examples of polysaccharides and how they are formed?

A
  • Glycogen is formed by the condensation of alpha glucose molecules.
  • Starch is formed by the condensation of alpha glucose molecules.
  • Cellulose is formed by the condensation of beta glucose molecules.
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12
Q

The chains formed from polysaccharides may be:

A
  • Branched or unbranched
  • Folded (making the molecule compact which is ideal for storage e.g. starch and glycogen).
  • Straight (making the molecules suitable to construct cellular structures e.g. cellulose) or coiled.
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13
Q

What is the structure and function of Glycogen?

A
  • It’s the main energy storage molecule in animals.
  • It’s a multi-branched alpha glucose polymer - joined by 1,4 and 1,6 glycosidic bonds.
  • Large number of branches (so energy can be released quickly as enzymes can act simultaneously on these branches).
  • Is stored in the muscles and liver
  • In times of high energy usage the muscles and liver hydrolyse the glycogen stored and break it down to glucose molecules which can be used in respiration.
  • Relatively large but compact molecule which maximises the amount of energy it can store.
  • It’s insoluble so it doesn’t affect the water potential of cells and can’t diffuse out of cells.
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14
Q

What is starch?

A

It’s a mixture of two polysaccharides called amylose and amylopectin. Both amylose and amylopectin are long-chain a-glucose polymers. Starch is the main form of carbohydrate used for energy storage in plants. Starch grains are stored in chloroplasts and are insoluble in water so they don’t affect water potential up and down the xylem - important for water and nutrient transport in the plant.

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15
Q

Structure of Starch:

A

It consists of two different polysaccharides:
Amylose (10-30%) - Unbranched helix-shaped chain with 1,4 glycosidic bonds between a-glucose molecules. The helix shape enables it to be more compact and thus it’s more resistant to digestion.
Amylopectin (70-90%) - 1,4 glycosidic bonds between a-glucose molecules but also 1,6 glycosidic bonds form between glucose molecules creating a branched molecule.

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16
Q

Properties of amylose:

A

Branches - Long, unbranched chains
Bonding - 1,4 glycosidic bonds
Shape - Chains coil into a helical shape

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17
Q

Properties of amylopectin:

A

Branches - Shorter chains, branched
Bonding - 1,4 and 1,6 glycosidic bonds
Shape - Branches out

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18
Q

What is cellulose?

A

Cellulose is a polysaccharide found in plants. It consists of long chains of b-glucose joined together by 1,4 glycosidic bonds. B-glucose is an isomer of a-glucose, so in order to form the 1,4 glycosidic bonds consecutive B-glucose molecules must be rotated 180 degrees to each other.

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19
Q

Structure and function of cellulose:

A
  • Highly abundant in cell walls, making it one of the most common molecule on Earth.
  • Unbranched, linear chains of b-glucose molecules which are joined by glycosidic bonds in a condensation reaction.
  • Polymer of about 10,000 b-glucose molecules in a long unbranched chain called a microfibril.
  • Microfibrils are strong threads which are made of long cellulose chains running parallel to one another that are joined together by hydrogen bonds forming strong cross linkages.
  • High stability due to the structure.
  • Adjacent glucose units are in opposite direction.
  • It’s important in stopping cell wall from bursting under osmotic pressure. This is as it exerts inward pressure that stops the influx of water, meaning, the cells stay turgid and rigid, helping to maximise the SA of plants for photosynthesis.
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20
Q

What is the test for reducing sugars?

A
  • Label 4 boiling tubes and place 4cm3 of the corresponding samples into each using fresh syringe each time.
  • Add 2cm3 of Benedict’s to each sample
  • Record the observations of each sample immediately
  • Place all 4 boiling tubes into the water bath
  • After 2 minutes record your observations of each sample, putting back the samples in the water bath after.
  • After another 2 minutes remove the tubes from the water and record final observations.
  • If the sample is a reddish colour it contains reducing sugars, if not it will be a blueish colour.
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21
Q

What is the test for non-reducing sugars?

A
  • After carrying out the reducing sugars test, use the negative samples
  • Put 4cm3 of each sample into a new test tube and add 2cm3 of 2moldm-3 hydrochloric acid to each of the samples.
  • Place all test tubes into the water bath and incubate for 2mins then take them out and let them cool.
  • Next neutralise the acid by adding sodium hydrogen carbonate to each sample until no more effervescence is observed.
  • Check the pH with indicator paper. If the pH is still lower than pH7, repeat the last step.
  • Add 2cm3 of Benedict’s to each of the samples
  • Record the observations immediately after and place all boiling tubes into the water bath.
  • After 2 mins, record your observations and after another 2 mins remove them from the water and record your final observations.
  • If non-reducing sugars are present the solution will turn reddish-brown and if it turns blueish then they aren’t present.
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22
Q

‘A red precipitate shows that a reducing sugar is present, with NO indication of the exact amount’ does this show a semi-quantitative, qualitative or quantitative method?

A

Qualitative

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23
Q

‘If you weighed the amount of copper oxide precipitate then this would give you a numerical value for the amount’ does this show a semi-quantitative, qualitative or quantitative method?

A

Quantitative

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24
Q

‘The more colour changes seen on heating with Benedict’s, the more sugar can be estimated to be in the sample being tested’ does this show a semi-quantitative, qualitative or quantitative method?

A

Semi-quantitative

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25
Q

Properties of lipids:

A
  • They contain carbon, hydrogen and oxygen
  • The proportion of carbon to oxygen and hydrogen is smaller than in carbohydrates
  • They are insoluble in water
  • They are soluble in organic solvents like alcohols, acetone and hexane
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26
Q

Function of lipids: (HINT: SHIPS)

A
  • Storage of energy for long-term use (e.g. triglycerides)
  • Hormonal roles (e.g. steroids such as oestrogen and testosterone)
  • Insulation - both thermal (triglycerides) and electrical (sphingolipids)
  • Protection of internal organs (triglycerides and waxes)
  • Structural components of cells (phospholipids and cholesterol)
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27
Q

What are the main lipid types?

A
  • Triglycerides and phospholipids
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28
Q

How are triglycerides formed with an explanation?

A

When condensation reactions occur between one glycerol and three fatty acid chains they are formed.

The hydroxyl groups of glycerol combine with the carboxyl groups of the fatty acids to form an ester linkage. This condensation reaction results in the formation of three molecules of water. During breakdown, these ester bonds are broken down by hydrolysis.

This also means when one triglyceride forms, three water molecules are released.

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29
Q

Describe saturated fatty acids:

A

These are fatty acids that possess no double bonds. This generates fats that are usually solid at room temperature. Saturated fatty acids are linear in structure, originate from animal sources and are typically solid at room temperatures.

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30
Q

Describe unsaturated fatty acids:

A

Fatty acids with noble bonds are unsaturated - either monounsaturated or polyunsaturated (>1 double bond). Unsaturated fatty acids are bent in structure, originate from plant sources (i.e. oils). Unsaturated fatty acids are usually liquid at room temperature and are called oils.

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31
Q

Describe the structure of a phospholipid:

A

In its hydrophilic head contains the phosphate group and the phosphoester bond. In the hydrophobic tail, the phosphoester bond connects to the glycerol. The glycerol forms ester bonds with the fatty acids. As phospholipids have both hydrophobic and hydrophilic parts they are amphipathic. Due to this, phospholipid molecules form monolayers or bilayers in water.

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32
Q

Describe the function of phospholipids:

A
  • Forming the plasma membrane of cells
  • In an aqueous environment being polar means a bilayer can be formed
  • The form the bilayer with the FA tails facing each other and the polar heads facing outwards.
  • Their structure allows them to form glycolipids with carbohydrates which are important on the cell surface membrane for cell recognition.
  • They are ideal for forming cell surface membranes as they enable integration of other molecules into the ‘mosaic’ and help regulate the movement of molecules in and out of the cell.
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33
Q

Describe the function and structure of cholesterol:

A

Cholesterol is manufactured primarily in the liver and intestines. It has a 4 carbon ring structure with a hydroxyl group at one end. Cholesterol is important in the formation and fluidity of cell surface membranes and in the production of certain hormones e.g. testosterone.

(Sterols (steroid alcohols) are another type of lipid found in cells)

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34
Q

Describe Low density lipoproteins (LDLs) and how they form:

A

Triglycerides (from fats sin our diet) combine with cholesterol and proteins to form LDLs which transport the cholesterol to our body cells.
LDLs carry cholesterol from the liver to the rest of the body. LDLs bind to receptors on cell surface membranes before being taken up by the cells where the cholesterol is involved in maintenance and synthesis of cell membranes. Excess LDL overload on these membrane receptors, results in high blood cholesterol levels, which can be deposited in the artery walls forming atheromas.

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35
Q

Describe High density lipoproteins (HDLs) and how they form:

A

HDLs are formed when triglycerides combine with proteins and cholesterol. They have a higher density because they have higher percentage of proteins and less cholesterol compared to LDLs. HDLs scavenge excess cholesterol in the body tissues and carry it back to the liver where it’s broken down which lowers blood cholesterol levels, and helps to remove the fatty plaques of atherosclerosis.

(think of ‘H’ for hoover - so they hoover the excess cholesterol in the arteries and carries to the liver where its broken down and passed through the body. So, LDLs raise blood cholesterol levels and HDLs lower blood cholesterol levels).

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36
Q

Why is it admirable to maintain a higher HDL:LDL ratio in the blood?

A

LDLs can form atherosclerotic plaques in the arteries whereas HDLs reduce blood cholesterol deposition. So, having higher HDL promotes excretion.

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37
Q

What are some dietary factors that increase cholesterol levels?

A
  • Saturated fats increase LDL levels within the body, raising blood cholesterol levels
  • Trans fats increase LDL levels and decrease HDL levels within the body, significantly raising blood cholesterol levels.
  • Unsaturated (cis) fats increase HDL levels within the body, lowering blood cholesterol levels
  • Saturated fats: they increase HDL and LDL but more LDL cholesterol
  • Monounsaturated fats: Helps removal of LDLs from the blood
  • Polyunsaturated fats: Increase LDL receptor site activity so the LDLs are actively removed from the blood.
38
Q

Describe the test for lipids:

A
  • Add a few drops of each liquid into different test tubes and add 2cm3 ethanol to each and shake thoroughly.
  • Add 2cm3 distilled water to each sample and shake gently to mix then observe and record the appearance.
  • Place a small piece of each solid sample into its own tube and add 2cm3 of ethanol to each sample.
  • Mash each sample using a glass rod and shake each tube thoroughly
  • Let the solid settle to the bottom of the tube and carefully pipette the ethanol from each sample into a fresh tube leaving the solid behind
  • Add 2cm3 of distilled water and shake gently to mix, observe and record the appearance of each.

If lipids are present it will appear cloudy white and if not it will be colourless.

39
Q

What are nucleotides?

A

Nucleotides are monomers which are the building blocks of DNA.

40
Q

There are 5 different nucleotides but what is the basic structure within all of them?

A

They all have:
- a ribose sugar joined to
- a phosphate group
- a nitrogen-containing base

41
Q

The bases change according to the nucleotide. What are they?

A
  • Guanine
  • Thymine (DNA only) or Uracil (RNA only)
  • Adenine
  • Cytosine
42
Q

What’s the difference between the types of nitrogenous bases (purines and pyrimidines)?

A

Purine bases form double ring structures whilst pyrimidine bases form single ring structure.

43
Q

How does the process of joining of nucleotides work?

A
  • The nucleotides bond between the phosphate group of one nucleotide and the sugar of another nucleotide. This is via a condensation reaction and the formation of a phosphodiester bond (consisting of the phosphate group and 2 ester bonds).
  • The chain of sugars and phosphates is known as the sugar-phosphate backbone.
  • Polynucleotides can be broken down into nucleotides again by breaking the phosphodiester bonds (through hydrolysis)
44
Q

How are base pairs joined together?

Which ones pair to which?

A

Two polynucleotide chains of DNA are held together via hydrogen bonding between complementary nitrogenous bases. But in order for the bases to be facing each other, the strands must be running in opposite directions. Thus, the two strands of DNA are described as being anti-parallel.

Thymine/Uracil pairs with Adenine with 2 hydrogen bonds.
Cytosine pairs with Guanine with 3 hydrogen bonds.

45
Q

What is the common basic structure of amino acids?

A
  • An amine (amino) group (-NH2) attached to a C atom
  • A carboxylic acid group (-COOH)
  • A hydrogen atom
  • A variable side chain (there are 20 so there’s 20 different amino acids)
46
Q

How does the dipeptide formation occur?

A

Amino acids are covalently joined together in a condensation reaction to form a dipeptide and the release of a water molecule. The covalent bond between the amino acids is called a peptide bond and so long chains of covalently bonded amino acids are called polypeptides.

47
Q

What is formed between two adjacent amino acids?

A
  • The amine group loses a hydrogen atom and the carboxylic acid loses a hydroxyl group forming water.
  • The removal means the C and N bond together forming a dipeptide.
48
Q

Define polypeptide:

A

A long chain of two or more amino acids joined by peptide bonds.

49
Q

Describe what’s in the primary structure of a protein:

A

It withholds the specific sequence and number of amino acids in a protein. The primary structure of a protein is determined by the gene.

50
Q

Describe what’s in the secondary structure of a protein:

A

The secondary structure that the chain of amino acids chains - either an alpha helix or beta pleated sheet.
Both a-helices and b-pleated sheets result from hydrogen bonds forming between non-adjacent amine and carboxyl groups.

a-helices are strong and helical in shape
b-pleated sheets are weak but strength is achieved through layering and bonds between layers.

51
Q

Describe the tertiary structure of a protein and what bonds are formed to maintain the structure:

A

Tertiary structures of proteins are the 3D shapes of the protein and is formed from further twisting and folding.
The following bonds are formed to maintain the structure:
- Disulphide bridges - Interactions between the sulfur in the R group of the amino acid cysteine, these are strong and not easily broken.
- Ionic bonds - form between the carboxyl and amino groups that are not involved in the peptide bond. They are easily broken by pH and are weaker than disulphide bridges.
- Hydrogen bonds (numerous and easily broken)
- Hydrophilic/hydrophobic interactions

not all proteins have a tertiary structure

52
Q

Why does the tertiary structure determine its function?

A

A polypeptide chain will fold differently due to the interactions between R groups.
Each of the twenty amino acids that make up proteins has a unique R group and therefore many different interactions can occur creating a vast range of protein configurations and so functions.

53
Q

Describe the quaternary structure of a protein?

A

It forms when two or more polypeptides come into contact. For example Haemoglobin. They usually have 4 sub-chains. The quaternary structures can be fibrous or globular.

54
Q

What is a conjugated protein?

A

A conjugated protein is a globular protein that contains a non-protein component called a prothetic group.

55
Q

What are proteins called without a prothetic group?

A

Simple proteins

56
Q

What ion do prosthetic groups contain and give an example of a prosthetic group?

A
  • Iron (II) ion
  • Haemoglobin
57
Q

What’s the function of haemoglobin?

A

It transports oxygen around the body in the red blood cells.

58
Q

Describe the structure of haemoglobin?

A
  • Globular conjugated protein
  • It’s made up of 4 polypeptide chains (2 a-subunits and 2 b-subunits)
  • Each of the four polypeptide chains in haemoglobin has a prosthetic group (being Haem)
  • A Haem group contains iron, which oxygen binds to
  • It has hydrophobic groups in the inside and hydrophilic groups on the outside
  • Quaternary protein
  • 2 alpha and beta chains with similar proportion of glycine to other amino acids
  • The Iron (II) ions present in the ham groups are able to combine reversibly with an O2 molecule.
59
Q

Describe globular proteins:

A
  • They roll up to form balls
  • They are soluble (as any hydrophobic R groups turn inwards and any hydrophilic R groups turn outward)
  • Usually have metabolic roles
  • Examples: Enzymes, plasma proteins, antibodies, some hormones (insulin), haemoglobin
60
Q

Describe fibrous proteins:

A
  • Form fibres in regular and repetitive sequences of amino acids
  • Usually insoluble
  • Usually have structural roles
  • Examples: Collagen, Keratin
61
Q

What are fibrous proteins?

A

Fibrous proteins are generally composed of long, narrow strands and have a structural role. E.g. Collagen, keratin and elastin

62
Q

What are collagen’s properties and describe its structure?

A

Properties: strong, tough and insoluble
Structure: Fibrous protein, a connective tissue found in skin, tendons, ligaments and the nervous system, one molecule of collagen is made up of 3 polypeptide chains twisted around each other in a long, strong rope-like structure and it’s flexible.

63
Q

Describe Keratin:

A
  • Its a group of fibrous proteins found in skin, nails, hair
  • Contains large proportion of sulphur containing amino acid Cysteine
  • This results in the formation of many strong disulphide bonds, forming strong, inflexible and insoluble materials.
  • Degree of disulphide bonds determine the flexibility of the protein (e.g. hair has few disulphide bonds whilst nails have more (becoming less flexible))
64
Q

Describe Elastin:

A
  • Fibrous protein
  • Found in elastic fibres
  • Present in the walls of blood vessels and in the alveoli of the lungs
  • Elastin gives these structures the flexibility to expand when needed
  • Quaternary protein
  • Made from many stretchy molecules called tropelastin
65
Q

Describe the process of continuous replication:

A

DNA polymerase always moves along the template strand in the same direction. It can only bind to the 3’ (OH) end, so travels in the direction of 3’ to 5’. As DNA only unwinds and unzips in one direction, DNA polymerase has to replicate each of the template strands in opposite directions. The strand that is unzipped from the 3’ end can be continuously replicated. This strand is called the leading strand and is said to undergo continuous replication.

66
Q

Describe the process of discontinuous replication:

A

The other strand from the replication process is unzipped from the 5’ end, so DNA polymerase has to wait until a section of the strand has been unzipped and then work back along. This results in DNA being produced in sections, called Okazaki fragments. These fragments then have to be joined. This strand is called the lagging strand and is said to undergo discontinuous replication.

67
Q

What does DNA helices do during DNA replication?

A

DNA helices unwinds and unzips the DNA by breaking the hydrogen bonds between bases.

68
Q

What does DNA polymerase do during DNA replication?

A

DNA polymerase links the newly arrived nucleotides by forming covalent bonds between phosphates and sugars. It only does this if the nucleotides are correctly paired.

69
Q

What does DNA ligase do during DNA replication?

A

DNA ligase joins together fragments of newly synthesized DNA to form a seamless strand.

70
Q

What is a gene?

A

A length of DNA that codes for a polypeptide or for a length of RNA that is involved in regulating gene expression.

71
Q

What’s the advantage of having different codes for the same amino acid?

A

A mutation may have no effect on the amino acid coded for as it can still be made in alternative ways.

72
Q

What is a triplet-code/codon?

A

The three nitrogenous bases read along the DNA strand that code for amino acids.

73
Q

Describe and explain the nature of the genetic code

A
  • Genetic code is universal as in almost all living organisms the same triplet of DNA bases codes for the same amino acid
  • Genetic code is degenerate as for all amino acids (except methionine and tryptophan) there’s more than one base triplet.
  • The genetic code is non-overlapping and its read starting from a fixed point in groups of three bases. If a base is added or deleted it causes a frame shift, causing disruption.
74
Q

Why is DNA replication described as semi-conservative?

A

Semi-conservative means ‘half the same’. When DNA replicates the double helix unwinds into twi separate strands; free nucleotides pair with their complementary bases; two new molecules of DNA are produced; each with one old strand and one new strand.

75
Q

Explain how polypeptides are synthesised through transcription and translation of genes

A
  • Genes are inside the cell nucleus but proteins are made in the cytoplasm, at ribosomes.
  • As the instructions inside the genes, on chromosomes, cannot pass out of the nucleus, a copy of each gene has to be transcribed into a length of mRNA.
  • In the form of mRNA, the sequence of bases (codons), can pass out the nucleus to the ribosome, ensuring that the coded instructions are translated and the protein assembled correctly from amino acids.
76
Q

Describe the process of transcription

A
  • RNA polymerase attaches to the DNA (The hydrogen bonds between the two DNA strands in the gene break, separating the strands and the DNA molecule begins to uncoil at this point. One of the strands is used as a template strand to make the mRNA copy)
  • Complementary mRNA is formed
  • RNA polymerase moves down the DNA strand ( The RNA polymerase moves along the DNA, assembling the mRNA strand. The hydrogen bonds between the uncoiled strands of DNA re-form once the RNA polymerase has passed by and the strands coil back into a double helix.
  • mRNA leaves the nucleus (It will inhibit protein synthesis)
77
Q

Describe the process of translation

A
  • mRNA attaches to ribosome (mRNA attaches itself to a ribosome at its start codon and transfer RNA (tRNA) molecules carry amino acids to the ribosome.
  • tRNA molecule attaches to mRNA (a tRNA molecule, with an anticodon that’s complementary to the start codon on the mRNA, attaches itself to the mRNA by complementary base pairing. A second tRNA molecule then attaches itself to the next codon on the mRNA in the same way)
  • rRNA joins amino acids (Ribosomal RNA in the ribosome catalyses the formation of a peptide bond between the two amino acids attached to the tRNA molecules. Joining the amino acids together and the first tRNA molecule moves away, leaving the amino acid behind).
  • Chain keeps forming until stop codon (A third tRNA molecule comes to bind to the next codon on mRNA. its amino acid binds to the first two, and the second tRNA molecule moves away. This process repeats continuously until a stop codon on the mRNA molecule)
  • Translation is complete (Polypeptide chain moves away from the ribosome)
78
Q

Describe the roles of RNA

A
  • RNA is a single-stranded polynucleotide, which means its made up of a number of RNA nucleotide molecules joined to each other with covalent bonds that form by condensation reactions.
  • RNA forms relatively short lengths of up to a few thousand nucleotides
  • 3 types of RNA: mRNA (messenger), tRNA (transfer), rRNA (ribosomal)
79
Q

Describe the roles of mRNA

A
  • mRNA is made in the nucleus during transcription
  • mRNA carries the genetic code from the DNA in the nucleus to the cytoplasm, where it’s used to make a protein during translation. its small enough to leave nuclear pores.
  • In mRNA, groups of three adjacent bases are called codons

mRNA contains uracil instead of thymine

80
Q

Describe the roles of tRNA

A
  • tRNA is folded into a clover shape. Hydrogen bonds between specific base pairs hold the molecule together in this shape.
  • Every tRNA molecule has a specific sequence of three bases at one end called an anticodon
  • They also have an amino acid binding site at the other end
  • tRNA is found in the cytoplasm where it’s involved in translation. It carries the amino acids that are used to make the proteins in the ribosome.
81
Q

Describe the roles of rRNA

A
  • rRNA forms the two subunits in a ribosome, along with proteins
  • The ribosome moves along the mRNA strand during protein synthesis
  • The rRNA in the ribosome helps to catalyse the formation of peptide bonds between the amino acids
82
Q

What are the two main types of cell respiration and how they link to ATP?

A
  • Anaerobic respiration involves the partial breakdown of glucose in the cytosol for a small yield of ATP
  • Aerobic respiration utilises oxygen to completely break down glucose in the mitochondria for a larger ATP yield
83
Q

What is ATP?

A

Adenosine triphosphate is the energy-carrying molecule that provides the energy to drive many processes inside living cells.

84
Q

Why do plants need energy?

A
  • Photosynthesis
  • Active transport (e.g. to take in minerals via their roots)
  • DNA replication
  • Cell division
  • Protein synthesis
85
Q

Why do animals need energy?

A
  • Muscle contraction
  • Maintenance of body temperature
  • Active transport
  • DNA replication
  • Cell division
  • Protein synthesis
86
Q

Functions of ATP:

A
  • ATP is the energy currency for the cell
  • ATP stores energy for the cell and releases it when energy is needed.
87
Q

What’s the reaction to form ATP?

A

ADP + Pi (inorganic phosphate) + energy <—-> ATP

88
Q

Uses of ATP: (hint:BANGME)

A

Biosynthesis of macromolecules (polymer assembly)
Active transport (endocytosis/exocytosis)
Nerve transmission (propagation of action potentials)
Growth and repair (mitotic division)
Movement (muscle contraction)
Emission of light (bioluminescence)

89
Q

Why is ATP a good energy source?

A
  • It stores or releases small amounts of energy at a time so no energy is wasted as heat
  • Can transfer energy by transferring a phosphate group
  • Small and soluble - easily transported around the cell
  • Easily broken down so energy can be released easily and rapidly
  • Can’t pass out of a cell so the cell always has a supply of energy
  • Made and re-made quickly
90
Q

Where does the energy needed to create ATP from ADP come from?

A

The breakdown of glucose in respiration

91
Q
A