Week 1 part 2 Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Protein

A

Linear polymer of a.a. joined by peptide bond (polypeptide)

Made by translation mRNA transcribed from genomic DNA

Biologic point of DNA/RNA allow synthesis of specific protein

Functions of P r determined by overall shape

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

Scale

A

Genome-DNA
|
v
P primary structure (Sequence)
|
v
P 3D structure
|
v
Function
|
v
Cell biology

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

Hydrophobic vs hydrophilic

A

Hydrophilic:
Polar electronic charge distribution (might carry a net +/- charge)
Interact well w/ polar solvent water

Hydrophobic:
Non-polar chain distribution
Do not interact well as polar solvent water
-Hydrophoic effect

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

Hydrophobic effect

A

WAter molecule adopt a constrained (cage-like) organization

If hydrophobic molecule coalesce, the # of water molecule is reduced(less water when hydrophobic mol. is bigger)

Lower intropy–>Higher entropy

“oil drop”=impo becasues cytoplasm is an aqueous solution… each protein has only one structure… if there’S more=conformations

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

What determined the path of the peptide backbone (shape of mol.)

A

2ndary and tertiary structure

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

The molecular structure of protein

A

Primary (sequence)

Secondary (local folding and hydrogen bonding… involve peptide backbone)

TErtiary (overall conformation)

Quaternary (multimetric structure=many polyp)

Supramolecular (large-scale assembly… they can assemble and unassemble)

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

Function of Protein

A

Determined by structure

Structure
Movement
Molecular transformation
Transport
Signaling
Binding
Catalysis
REgulation

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

Primary structure

A

A.A. squence determine structure and function
so DNA inderctly determin the P function

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

SEcondary structure

A

only looking at backbon(no side chain)

a helix and B sheet

both r based on H-bonding between

peptide bond carbonyl O atoms one aminio residue
&
amino group hydrigens on a diff. amino acid residue

60% of P corrsponds to these structure… others have a definite one but not those

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

a-helix

A

Periodicity of 3.6 residue/turn (titlted axis)
…every 36 a.a.=10 turn…

H-bond between N and N+4

Gross structure straight rod

Surface properties depend on side chain becasue they are the one that interacts with other part of P… so it is there that the propensity for the helox to form is decided

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

B-sheet

A

H-bond between 2 adj. B-strands

Can creat large surface

Side chai=above and below sheet’S plane and they determine the propensity of the sheet to form by interactin with other part of the P

Antiparallel or parallel

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

Tertiart structure

A

OVerall conformation of the polypeptide (spatial organization of the multipel secondary structure element)…ex: a-helix+B-sheet+side chains

Amino acid side-chain mediate interaction (non-convalent)
between diff. part of the P and between the P and its lgand GDP

IMPO: COVALENT BOND: CYSTEINE

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

Cysteine

A

Contains a sulfhydryl group that form convalent S-S(disulfide) bonds w/ other cysteine side chains

In P, disulfide bonds can be intrachain (teritary structure) or interchain (quaternary structure)

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

Quaternary structure

A

Check image

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

Motids of P structure

A

Coiled-coil motif

EFhand/helix-loop-helix-motif

Zinc-finger motif

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

Coiled-coil motif

A

Comb of 2 a-helix
Hydrophobic side-chain dacing each other inside (oil drop)

Heptad reapeat:
HxxHxxxHxxHxxx
(every 7 residues=2 Hydrophobic)

7/2=3.5 (vs pitch helix 3.6)

Involved in P interactions

17
Q

EFhand/helix-loop-helix motif

A

2 a-helix at 90°
w/ loop of a.a. between them

A Ca2+ binding motif

18
Q

Zinc-finger motif

A

a-helix + 2 B-sheet

Common in transcription factors (binds to DNA/RNA)

Side chain binding w/ Zn

19
Q

Motifs vs domains

A

Motif is not a whole P (too small)…
it has to be embedded in smthg holding it tgtr (NOT STRUCTURALLY INDEPENDANT)

Domain(larger(: 40 a.a. + contain 2ndary struc.

have enought bonds to hold itself tgtr even if cut out from P (compactly folded),
can be made of manny motifs (STRUCTURALLY INDEPENDANT ENTITIE)

20
Q

4 major structural classes of P

A

Fibrous protein: fibesr

Globular protein (oild rop)

Integral membrane proteins (hydrophobic region)

Intrinsically disorded P: random coils under physiological conditions… may adop specefic 2/3 stru. upon binding to a well structured partner P

21
Q

Molecular nature of P domain

A

Domains can be found in unrelated P