Lecture 8 - Protein Structure from primary to quaternary Flashcards

1
Q

what is the primary structure of a protein?

A

-amino acid sequence in a polypeptide chain

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2
Q

what is the secondary structure of a protein?

A

-helix

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3
Q

what is the tertiary structure of a protein?

A
  • one complete protein chain

- beta chain of hemoglobin

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4
Q

what is the quaternary structure of a protein?

A

-the four separate chains of hemoglobin assembled into a oligomeric protein

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5
Q

what is the second level of protein structure dictated by?

A

hydrogen bonds between nearby residues

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6
Q

what are protein folds made up of?

A

secondary structural motifs interrupted by loops

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7
Q

how can secondary motifs be identified?

A

from backbone torsion angle distributions

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8
Q

What do backbone torsion angles describe?

A

-the twisting of the protein peptide backbone

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9
Q

Why is the — angle almost always 180?

A

peptide bond has special resonance structure

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10
Q

What does a Ramachandran plot show?

A

(..,..) angle distribution in a protein

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11
Q

what are alpha helices?

A

right-handed coils

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12
Q

how many residues per turn in an alpha helix?

A

average 3.6 residues per turn

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13
Q

What is the average alpha helix lenght?

A

12 residues, ~3 turns

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14
Q

are beta sheets parallel or antiparallel?

A
  • can be both

- anti parallel sheets occur more frequently

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15
Q

What is a quality of an antiparallel sheet?

A

-pleated with repeated distance averaging 7.0

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16
Q

What do helices and sheets form?

A

-a continuum

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17
Q

which amino acids favor alpha helices?

A
ala
cys
leu
met
glu
gln
his
lys
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18
Q

which amino acids favor beta sheets?

A
val
ile
phe
tyr
trp
thr
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19
Q

which amino acids favor turns?

A
gly
ser
asp
asn
pro
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20
Q

What is the difference between fibrous and globular proteins?

A

globular proteins: compact + tightly folded

fibrous proteins: elongated, dominated by helices

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21
Q

what do fibrous proteins serve mostly as?

A

structural elements

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22
Q

what is alpha keratin?

A

coiled coil

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23
Q

what is keratin?

A

-principal component of hair, horn, nail + feathers in birds/animals

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24
Q

what is keratincomposed of?

A

-long alpha helix

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25
what do two keratins form?
- hydrophobic interactions to form a coiled coil | - keratin dimer coiled coil
26
what is collagen?
triple helix
27
collagen is the most _______ in ____
- abundant protein | - vertebrates
28
What is collagen the main component of?
bone, teeth, cartilage, tendon, skin, blood vessels
29
how is hydroxyproline made?
- by modifying prolines after the collagen fiber is assembled - requires vitamin C
30
what are 2 methods used to determine tertiary structures?
1. X-ray | 2. NMR
31
what is X-ray?
-differaction method
32
What does X-ray require?
crystal of the protein
33
what does X-ray reveal?
-electron density contours of the molecule
34
what is the structure of a protein in solution identical to?
-largely identical to its crystal structure
35
what is NMR?
- nuclear magnetic resonance | - solution-based method
36
What does NMR measure?
distances between H atoms on the protein
37
what does NMR usually contain?
-ensemble of structures
38
what is the key determinant of side chain locations?
-hydrophobicity
39
AA with nonpolar side chains
``` val ile leu met phe (occur mostly on inside) ```
40
AA with charged side chains
``` arg lys his asp glu (mostly occur on outside) ```
41
AA with polar side chains
``` ser thr asn gln (usually on surface, can be see on inside) ```
42
what do tertiary structures contain?
-combinations fo secondary motifs
43
larger proteins have ______
multiple domains
44
what is a quality of multiple domains in larger proteins?
-each domain folds like a separate unit and has a distinct function
45
are domains the same as subunits?
NO -domains: on same chain -subunits: on different chains
46
what do quaternary structures describe?
how subunits are packed
47
how are subunits assembled?
by van der Waals interactions
48
for identical or near-identical subunits there is often _____
an overall symmetry
49
what are 4 factors involved in the stability of protein folds?
1. hydrophobicity 2. disulfide bonds 3. metal atoms 4. electrostatic interactions
50
Proteins can undergo ____ and _____
denaturation and renaturation
51
what are 2 common denaturants?
1. Guanidinium ion | 2. urea
52
what are the 5 steps of denuration?
1.
53
what are conformations?
-the different geometries the protein can fold into
54
when does the protein have highest conformational entropy?
in its unfolded state
55
What is the entropy of a protein when it is in its unfolded state?
-the protein has highest conformational entropy
56
what is the folding funnel?
-hierarchical pattern of folding
57
what does the folding funnel say about structure and entropy?
...
58
what happens to proteins as they are being synthesized in the ribosome?
they fold
59
what accelerates S-S interchanges?
disulfilde isomerase
60
what does disulfide isomerase do?
accelerates S-S interchanges
61
what is the GroEL-GroES chaperonin complex?
an ATPase motor protein
62
what do chaperone proteins do?
help correct misfolding
63
what are the 4 steps of a chaperone protein?
1.