Proteins/protein structure 1 Flashcards

1
Q

four levels of protein structure

A

primary
secondary
tertiary
quaternary

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

protein classification by shape

A

globular vs fibrous

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

protein classification by composition

A

simple vs conjugated

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

contain only amino acids

A

simple proteins

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

contain protein and ‘non protein’ components

A

conjugated proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

the specific amino acid sequence of a protein

A

primary structure

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

similar sequence and arose from the same ancestor gene, and carry out similar fuctions

A

homologous proteins

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

sickle cell anemia is caused by a substitution of _____ for a ____

A

valine for a glutamate

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

polypeptide bond between nitrogen on amino group and alpha carbon

A

phi bond

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

polypeptide bond between alpha carbon and carboxyl carbon

A

psi bond

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

polypeptide bond between carboxyl carbon and nitrogen of amino group

A

omega bond

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

structures stabilized by hydrogen bonding between carbonyl and the N-H groups of polypeptide’s backbone

A

secondary structure

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

two most common secondary structures

A

alpha helix

beta pleated sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

a rigid, rod-like structure formed by a helical turn

A

alpha helix

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

alpha helix are stabilized by hydrogen bonding between N-H and a carbonyl group ____

A

four amino acids away

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

two amino acids that do foster alpha helix

A

glycine

proline

17
Q

why doesn’t glycine form alpha helix

A

its to small and flexible

18
Q

why doesn’t proline form alpha helix

A

too rigid, lacks a N-H group for hydrogen bonding

19
Q

which are more abundant in nature left or right handed secondary structures

A

right handed secondary structures

20
Q

three different types of right handed alpha helices

A

alpha helix
3-10 helix
pi helix

21
Q

form when two or more polypeptide chain segments line up, side by side

A

beta pleated sheets

22
Q

two types of beta pleated sheets

A

parallel

antiparallel

23
Q

which type of beta sheet is less stable

A

parallel sheets

24
Q

many proteins have supersecondary structures with patterns of alpha helix and beta sheets

25
refers to unique three dimensional structures formed by globular proteins
tertiary structure
26
four main chemical interactions help stabilize tertiary structure
hydrophobic interactions ionic interactions hydrogen bonds covalent bonds
27
hydrophobic R groups are brought together as they exclude water or are excluded fro water
hydrophobic interactions
28
occurs between R goups of amino acids
hydrogen bonding
29
includes disulfide bridges
covalent bonds
30
occurs especially between oppositely charged groups
ionic interactions
31
structurally independent segments that have specific functions
domains
32
core structural element of a domain is
fold
33
proteins that consist of repeated domains
mosaic or modular proteins
34
level of structure achieved when two or more folded polypeptides in tertiary structure associate to form a functional protein
quaternary structure
35
individual polypeptides in quaternary structure are called
subunits
36
three reasons for common occurrence of multiunit proteins
1. synthesis of subunits is more efficient 2. worn out subunits can be replaced more effectively 3. biological function requires interaction of subunits
37
polypeptide subunits are held together by
linkages
38
covalent cross links in collagen are initiated by
lysyl oxidase
39
some proteins are partially or completely unstructured
unstructured proteins