Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BMS02 > Protein Structure & Function > Flashcards

Protein Structure & Function Flashcards

1
Q

What is the primary protein structure?

A

Sequence of amino acids in the polypeptide chain

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

What is the secondary protein structure?

A

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

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

What is the tertiary protein structure?

A

Polypeptide chain folds upon itself further

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

What is the quaternary protein structure?

A

Folded polypeptide chains join together

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

List the bonds present in proteins in ascending strength

A

Van der Waals

Hydrogen

Ionic

Covalent

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

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

A

Peptide bond resonance (delocalised electrons)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is the pitch of an alpha helix?

A

0.54nm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

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

A

3.6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What type of helix is an alpha helix?

A

Right handed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Where are the R groups of an alpha helix?

A

On the outside

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Where are the R groups in a beta pleated sheet?

A

Alternately above and below the plane of sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How long is one fold of a beta pleated sheet?

A

0.7nm

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What percentage of haemoglobin is made up of alpha helices?

A

60%

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

What is the most abundant protein in vertebrates?

A

Collagen

26
Q

What is the structure of collagen?

A

Triple helix - three left hand helices join to form a right hand helix (triangular)

27
Q

In collagen, how many residues are there per turn?

A

3

28
Q

What is the amino acid sequence of collagen?

A

Gly - X - Y - Gly - X - Y

X = mainly proline

Y = mainly hydroxyproline

29
Q

Where is type I collagen found? (4)

A

Skin

Bone

Tendon

Dentin

30
Q

Where is type II collagen found?

A

Cartilage

31
Q

Where is type III collagen found? (2/3)

A

Extensible tissue (blood vessels and lungs)

Dental pulp

(Minor component in dentin)

32
Q

What causes scurvy?

A

Vitamin C deficiency

33
Q

Explain why scurvy occurs.

A

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
Q

What are the symptoms of scurvy? (5)

A

Skin bruises easily

Old wounds reopen

New wounds heal poorly

Gums bleed

GI tract bleeding

BMS02 (10 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions