Protein structure dictates function Flashcards

1
Q

What determines the shape of a protein?

A

The sequence of amino acids

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2
Q

Name the levels of protein structure in order

A
Primary
Secondary
Tertiary
Quaternary
Supramolecular
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3
Q

What is primary structure?

A

Amino acid sequence

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4
Q

What is secondary structure?

A

Local folding

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5
Q

What is tertiary structure?

A

Long range folding

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6
Q

What is quaternary structure?

A

Multimeric organisation

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7
Q

What is supramolecular structure?

A

Large-scale assemblies

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8
Q

What is the Levinthal paradox?

A

Assuming each amino acid can be in 3 conformational states
A protein of 101 amino acids has 3^100 possible conformations
Clearly structure is not down to chance

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9
Q

What restricts the possible shape of a protein?

A

The chemical properties of atoms and the peptide bond

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10
Q

What constrains the folding of a protein?

A

Non-covalent interactions between amino acid side chains

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11
Q

Which two regular folding patterns are seen at the secondary level?

A

Alpha helix

Beta pleated sheet

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12
Q

Describe the bonds in an alpha helix

A

Intra-strand interactions of the amino acid backbone

Hydrogen bonds

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13
Q

Describe the bonds in a beta pleated sheet

A

Inter-strand interactions of amino acid side chains

Hydrogen bonds

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14
Q

What is the length it takes for one turn of an alpha helix?

A

0.54nm

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15
Q

What is the length it takes for one pleat of a beta pleated sheet?

A

0.7nm

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16
Q

What is important about the orientation of beta pleated sheets?

A

They run counter parallel to one another

17
Q

Which bond stabilises structures?

A

Hydrogen bonding

18
Q

What is a hydrogen bond?

A

The electrostatic attraction between polar molecules

19
Q

Which atoms can form hydrogen bonds?

A

Nitrogen
Oxygen
Fluorine

20
Q

How close together must two atoms be for a hydrogen bond to form?

21
Q

Which non-covalent interactions are present in proteins?

A

Ionic bonds
Hydrogen bonds
Van der Waals
Hydrophobic associations

22
Q

Which amino acids form ionic bonds?

A

Amino acids with carboxylic acid side chains

Amino acids with amine side chains

23
Q

What is important in the formation of ionic bonds?

24
Q

Give a basic explanation of van der Waals interactions

A

Electron cloud is constantly fluctuating
Small areas of charge created in an atom
Attraction or repulsion occurs

25
Van der Waals are only significant...
...when combined
26
When clustering of hydrophobic side chains occurs, it leads to...
...other non-covalent interactions | Because side chains are brought close enough together to interact
27
If there is a hydrophobic region on the exterior of a folded protein, what might be its function?
A contact site for other proteins | Once the subunits come together the hydrophobic region is away from the water
28
Which amino acid forms disulphide bridges?
Cysteine
29
Disulphide bridges are present in what structural level?
Quaternary
30
What do weak non-covalent interactions determine?
Geometry Specificity Kinetics
31
What is entropy?
Disorder | Everything is increasing towards a state of disorder
32
What is deltaG?
A measure of the change of free energy
33
What does a negative or positive value of deltaG mean?
Negative: releases energy, favourable Positive: requires energy, not favourable
34
What is deltaG in the context of protein folding?
The energy released or require when a protein folds into its native conformation
35
DeltaG is defined by
DeltaG = deltaH - TdeltaS where deltaH = enthalpy deltaS = entropy
36
What happens to the entropy of water as a protein folds?
When unfolded, water forms hydration spheres around hydrophobic side chains Entropy is decreased When protein folds, the water molecules are released Entropy is high
37
When a protein folds, energy is ______
Released
38
What is the deltaH value for protein folding?
Negative
39
What is the deltaG value for protein folding?
Negative | Favourable