Protein Structure & Function Flashcards

1
Q

What is the primary protein structure?

A

Sequence of amino acids in the polypeptide chain

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2
Q

What is the secondary protein structure?

A

Folding/coiling of polypeptide chain (alpha helix/beta pleated sheet)

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3
Q

What is the tertiary protein structure?

A

Polypeptide chain folds upon itself further

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4
Q

What is the quaternary protein structure?

A

Folded polypeptide chains join together

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5
Q

List the bonds present in proteins in ascending strength

A

Van der Waals

Hydrogen

Ionic

Covalent

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6
Q

List the types of hydrogen bond combinations in descending strength

A

F-H F

O-H N

O-H O

N-H N

N-H O

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7
Q

Why are there partial charges on the nitrogen and oxygen of a peptide bond?

A

Peptide bond resonance (delocalised electrons)

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8
Q

What is the pitch of an alpha helix?

A

0.54nm

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9
Q

How many amino acids are there per turn of an alpha helix?

A

3.6

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10
Q

What type of helix is an alpha helix?

A

Right handed

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11
Q

Where are the R groups of an alpha helix?

A

On the outside

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12
Q

Where are the R groups in a beta pleated sheet?

A

Alternately above and below the plane of sheet

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13
Q

How long is one fold of a beta pleated sheet?

A

0.7nm

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14
Q

What is the difference between a parallel and antiparallel beta pleated sheet?

A

Parallel = all chains run in same direction

Antiparallel = adjacent chains run in opposite directions

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15
Q

What percentage of haemoglobin is made up of alpha helices?

A

60%

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16
Q

What do silk fibres/fibrillar proteins (fibroin) contain a lot of?

A

Beta pleated sheets

17
Q

What is the super-secondary structure?

A

Common domains formed from combinations of alpha helices and beta pleated sheets found in many proteins

18
Q

What are ionic bonds/salt bridges?

A

Electrostatic attractions between charged side chains

19
Q

What is the main driving force for folding of soluble proteins?

A

Hydrophobic side chains (forming a hydrophobic core)

20
Q

On proteins spanning the lipid bilayer, where are the hydrophobic side chains?

A

Outside (hydrophilic core)

21
Q

What is O-linked glycosylation?

A

Addition of sugar onto the OH of Thr/Ser

22
Q

What is N-linked glycosylation? Give an example

A

Addition of sugar onto NH2 of Asn

SIBLING protein family = Small Integrin-Binding Ligand N-linked Glycoprotein

23
Q

What processes is phosphorylation of proteins involved in?

A

Cell signalling (phosphorylation of Tyr with insulin receptor)

Change in enzyme activity (phosphorylation of pyruvate kinase in response to blood glucose)

24
Q

Explain how acetylation affects DNA gene transcription.

A

Binds to Lys in histones to “remove” positive charge so negatively charged DNA is attracted less strongly and moves away

Increased transcription

25
What is the most abundant protein in vertebrates?
Collagen
26
What is the structure of collagen?
Triple helix - three left hand helices join to form a right hand helix (triangular)
27
In collagen, how many residues are there per turn?
3
28
What is the amino acid sequence of collagen?
Gly - X - Y - Gly - X - Y X = mainly proline Y = mainly hydroxyproline
29
Where is type I collagen found? (4)
Skin Bone Tendon Dentin
30
Where is type II collagen found?
Cartilage
31
Where is type III collagen found? (2/3)
Extensible tissue (blood vessels and lungs) Dental pulp (Minor component in dentin)
32
What causes scurvy?
Vitamin C deficiency
33
Explain why scurvy occurs.
Vitamin C = cofactors for proline hydroxylase No vitamin C means no hydroxylation of proline Resulting in unstable collagen as less hydrogen bonds can be formed
34
What are the symptoms of scurvy? (5)
Skin bruises easily Old wounds reopen New wounds heal poorly Gums bleed GI tract bleeding