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Advanced Higher Biology 2022 > Unit 1.2 - Proteomics > Flashcards

Unit 1.2 - Proteomics Flashcards

1
Q

What is the Proteome?

A

Entire set of proteins expressed from a genome

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2
Q

Why is the proteome bigger than genome?

A

Alternative RNA Splicing

Post Translational Modification

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3
Q

What are the two functional groups found in all amino acids?

A

Amine

Carboxylic Acid

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4
Q

What happens to an amino acid when it is in aqueous solution?

A

NH2 gains a hydrogen to become NH3+

COOH loses a hydrogen to become COO-

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5
Q

What are the four classes of amino acids?

A

Acidic
Basic
Polar
Hydrophobic

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6
Q

What class of amino acids are negatively charged?

A

Acidic

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7
Q

Describe the characteristics of a basic R group

A

Positively Charged
Functional group example: -NH2
Example: Lysine

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8
Q

What class of R groups are found at the surface of a protein?

A

Polar

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9
Q

What constitutes a peptide bond?

A

C, H, O, N

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10
Q

What is the primary structure of a protein?

A

Order in which the amino acids are synthesised into the polypeptide

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11
Q

What stabilises secondary structure of the protein?

A

Hydrogen Bonds

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12
Q

Where does the hydrogen bonding occur between in secondary structure?

A

N-H has a weak positive charge and C=O has a weak negative charge

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13
Q

What are the three types of secondary structure?

A

Alpha Helix
Beta Sheets
Turns

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14
Q

Where are the R groups facing in an alpha helix?

A

Outwards

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15
Q

Where are the R groups sitting in a beta sheet?

A

Above and Below

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16
Q

What are the two types of beta sheets?

A

Antiparallel and parallel

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17
Q

If chains run in opposite directions(in respect to N-C polarity) what type of beta sheet is it?

A

Antiparallel

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18
Q

What causes tertiary structure?

A

Interactions between R groups of amino acids

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19
Q

State some possible interactions between R groups

A

Ionic Bonds
Van der Waals
Disulphide Bridges

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20
Q

What is special about the R groups that are connected with disulphide bridges?

A

R groups contain sulphur

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21
Q

How does temperature affect the proteins?

A
  • Tertiary structure is destabilised, leading to denaturation
  • Increased heat = more kinetic energy, polypeptide chain shakes more
  • Weaker interactions such as H bonds are broken
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22
Q

How does pH affect the proteins?

A

Effects ionisation of the acidic and basic R groups
Changes the charge, so they no longer bond correctly
Polypeptide Unfolds

23
Q

What is Quaternary structure?

A

When more than one polypeptide sub-unit join together to form a protein

24
Q

Give an example of a protein with Quaternary structure

A

Collagen

Haemoglobin

25
What is co-operativity?
When ligand binding at one protein subunits alters the conformation of the other subunits
26
State three important functions of R groups
- Determine the structure of a protein - Allows the binding of ligands - Determines the location of proteins in the cell
27
How do cytoplasmic proteins become more soluble in aqueous solutions?
Greater proportion of hydrophyllic amino acids Prosthetic groups are added to increase hydrophyllic - ness Hydrophobic R groups cluster towards centre
28
How could you tell if a protein is not soluble?
If there is no net charge on the surface of the protein at the isoelectric point
29
What kind of molecules can pass through the membrane?
Non polar (small)
30
What acts as a barrier to charged ions and polar molecules passing through the membrane?
Hydrophobic centre
31
What are the two types of membrane proteins?
Integral and peripheral
32
What type of bonds do integral proteins form?
Hydrophobic bonds
33
Where do the integral membrane proteins interact?
Tails of the phospholipids
34
Describe the bonding of peripheral proteins to the membrane
form weak bonds with surface of the membrane
35
What is a ligand?
Substance that can bind to a protein
36
In what ways are the ligand binding sites complementary to the ligand?
Shape and chemistry
37
What is caused in the protein by a conformational change?
Functional Change
38
What charges do histones carry?
Positive
39
What charge is the sugar phosphate backbone of DNA?
Negative
40
State important roles of DNA binding
Help to form linear chromosomes | Regulating the transcription of genes
41
Describe induced fit
Small changes in bonding pulls the enzyme structure towards the substrate Increases interaction between active site and substrate Enzyme is trying to revert to original state Places the substrate under tension Lowers activation energy Once the experiment is completed the active site has less affinity for products Products are released Enzymes return to original confirmation
42
How can the rate of product formation in a metabolic pathway be regulated?
Raising or lowering the activity of an enzyme (allosetric enzyme)
43
What do positive modulators do?
Increase affinity and enzyme activity
44
How many polypeptide sub-units are there in haemoglobin?
4
45
What does each subunit of haemoglobin contain?
Haem
46
What is the function of Haem?
Allow for oxygen binding
47
What conditions reduce affinity of oxygen?
Low pH | High Temperature
48
What do inactive proteins need to become active?
Post Translational Modification
49
What is the most of common of activation?
The addition of a phosphate to R groups
50
What are Kinases?
Proteins that catalyse the process of phosphorylation
51
A protein catalyses dephosphorylation. What type of protein is this?
Phosphatases
52
What are ATPases?
Proteins that can cause their own conformational change by phosphorylating themselves.
53
What two conditions would increase the product yield of an enzyme reaction?
Adding a positive modulator | Increasing enzyme concentration

Advanced Higher Biology 2022 (16 decks)

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