exam 2 protein shape and structure Flashcards

1
Q

what is protein structure determined by

A

the sequence of amino acids

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

what can proteins be divided into

A

functional and structural domains

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

what are function and structural domains

A

independently folding subregions within the protein sequence

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

what determines a protein’s function

A

the 3D structure of it

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

what is primary structure of proteins

A

linear sequence of amino acid residues determined by the mRNA code

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

what is primary structure held together by

A

peptide bonds between amino acids

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

what determines higher order structures

A

protein structure in combination with a protein’s environment

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

what is the sequence of proteins different from

A

the sequence that initiates folding process

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

what is the secondary structure of a protein

A

the folding and twisting of peptide backbone

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

what is the secondary structure held together by

A

weak H-bonds between C=O (carbonyl) and N-H (amine) groups in the backbone

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

what do the two bonds of every amino acid have

A

the two bonds have freedom of rotation

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

what is the purpose of side chains in the secondary structure

A

they make it more or less difficult for structure to form, but don’t hold secondary structure together

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

what are the two secondary structures

A

alpha helices and beta sheets

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

what is the structure of the alpha helix

A

rigid cylindrical structure

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

when does an alpha helix form

A

forms when H-bonding occurs between a carbonyl and amine group that are 4 amino acids apart on the polypeptide backbone

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

what makes one turn of the helix

A

four amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what direction does coiling of the alpha helix happen in

A

a clockwise direction down the length of the chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

what is the beta sheet

A

a flat, folded, sheet-like structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

when does a beta sheet form

A

when H-bonding occurs between a carbonyl and amine group on adjacent polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what does it mean for an adjacent beta sheet chain to be parallel

A

adjacent chains run N-terminal to C-terminal

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what does it mean for an adjacent beta sheet chain to be antiparallel

A

adjacent chains run in opposite directions

22
Q

what do rigid proline residues do

A

insert a kink in a protein’s backbone and disrupt secondary structures

23
Q

what is tertiary structure of proteins

A

3D arrangement of secondary structures to assume the lowest possible energy state

24
Q

what is tertiary structure (detailed)

A

stretches of proteins that serve as links between secondary structures to allow them to fold up

25
what is tertiary structure held together by
non-covalent attractions between R-groups along with R-groups + the surrounding environment
26
what links secondary structures together to form tertiary structures
unstructured loops (aka random coils)
27
what can tertiary structure stabilized by
covalent interactions - most important are disulfide bonds
28
where can covalent disulfide bonds form to stabilize tertiary structures
between cysteine residues to cross-link parts of the polypeptide backbones
29
what does stabilizing tertiary structures do
makes it more difficult to unfold once it's in the shape
30
what is the difference is the energy of unfolded and folded proteins
unfolded proteins have a higher free energy than when it's folded due to entropy
31
what does protein stability depend on
the free energy change between the folded and unfolded states
32
what is delta G
G(folded) - G(unfolded) : products minus reactants
33
what charge creates the most stable folded protein
the most negative the change in free energy
34
what are molecular chaperones (chaperonins)
provide an isolated chemical environment in which they can fold, which proteins require to 3D fold
35
what is a prion
an infectious protein
36
what are prions evidence of
that some unusual contagious neurological diseases are caused by proteins alone
37
what happens when a prion protein interacts with a correctly folded protein
it recruits it to also fold incorrectly (ex: mad cow, kuru)
38
what is a protein domain
a region of the protein that folds essentially independently of other regions
39
how many protein domains can a protein have
single or multiple
40
what does a domain represent
a functional region of the protein - different domains have different function
41
what do catalytic protein domains do
inhibit host cell protein synthesis
42
what do hydrophobic protein domains do
inserts into the membrane
43
what do receptor binding protein domains do
attach to cell surface
44
what are motifs
similar domains that occur in many related proteins
45
what is quaternary protein structure
arrangement of multiple tertiary structures
46
what are quaternary structures held together by
weak bonds and some disulphide bonds
47
what are homomers of quaternary structures
identical subunit polypeptides
48
what are heteromers of quaternary structures
different subunit polypeptides
49
what is the final structure of a protein after quaternary structure
mature protein
50
what does a higher order structure increase
efficiency