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Biochemistry > L12 > Flashcards

L12 Flashcards

(76 cards)

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1
Q

R groups are attached to

A

Alpha C

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2
Q

Which type of bond in involved in HB?

A

Peptide bonds

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3
Q

Peptide bond is formed between

A

Alpha NH2 - alpha COOH

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4
Q

Huntington disease is caused by

A

Addition of Gln

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5
Q

Cystic fibrosis is caused by

A

Deletion of phe from CFTR protein

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6
Q

Sickle cell anemia is caused by

A

Glu —> val in B-globin

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7
Q

Which takes more time? DNA or protein sequencing?

A

Protein

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8
Q

These structures are found in every protein (1* ,2, 3, 4*)

A

1, 2

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9
Q

This structure is found in most proteins (1* ,2, 3, 4*)

A

3

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10
Q

is found in some proteins (1* ,2, 3, 4*)

A

4

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11
Q

Peptide bonds are in (1* ,2, 3, 4)
HB are in (1 ,2, 3, 4)
Ionic, covalent, HB, Hydrophobic are in (1 ,2, 3, 4*)

A

1
2
3,4

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12
Q

___ bond is stable, not broken by mild denaturants

A

Peptide bonds

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13
Q

Which structure has polarity? (1* ,2, 3, 4*)

A

1, from N—> C terminal

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14
Q

What is the direction of peptide syntheses?

A

N—>c

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15
Q

T/f: Primary structure is normally linear, but may be branched

A

T

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16
Q

Example of branched 1* structure

A

Insulin

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17
Q

How is the 1* structure determined?

A

by protein sequencing

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18
Q

What method is used to sequence proteins?

A

Sanger’s, a chemical method

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19
Q

Which method sequenced insulin chains

A

Sanger’s

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20
Q

Why do we sequence proteins

A

To understand biological structures and diseases

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21
Q

Protein sequencing always starts with which terminal?

A

N

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22
Q

Explain the protein sequencing mechanism

A

1) identify NH2 using PITC in BASIC PH
2) cleave the aa by PEPTIDE BOND ACID LABILE in ACIDIC PH
3) identify the cleave by HPLC/ chromatography

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23
Q

T/F: Sequence is obtained by identifying the N-terminus aa one by one

A

T

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24
Q

How are 2* formed ?

A

Interactions between aa residues THAT ARE CLOSE TO EACH OTHER IN THE POLYPEPTIDE

Local folding

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25
How are 2* stabilized?
HB
26
One turn in a-helix structure contains
3.6 aa
27
Rise per aa in a-helix
1.5A*
28
Side chains in a helix are extended__ While in B-sheet __
outwards Up, down
29
a-helix can be broken by heat and other denatures unlike __
Peptide bonds
30
Rare ?(a-helix a-helix3 pi-helix)
a-helix3 pi-helix)
31
Most relaxed (a-helix a-helix3 pi-helix)
a-helix3
32
Most condensed (a-helix a-helix3 pi-helix)
pi-helix
33
aa/ turn for (a-helix a-helix3 pi-helix)
3.6 3 4.4
34
HB between which aa in (a-helix a-helix3 pi-helix)
1-4 1-3 1-5
35
What are the aa that disrupts the a-helix
Proline: H❌ Glycine: too flexible
36
Mention the % of a-helix in (keratin, myoglobin, chymotrypsin)
100% 80% ~0%
37
Formed by bending of a polypeptide segment over another
B-sheet
38
Surface appears pleated
B-pleated sheet
39
B-sheet is stabilized by
HB
40
Is ridged
B-structure
41
Proline and glycine aa are incompatible or disrupt this structure
B-sheet
42
Formed by abrupt disruption of the β-sheet
B-turn
43
Reverses the direction of β-sheet
β-turn
44
Connects two successive B-sheets
B-turn
45
How many aa is B-turn made up of
4aa, proline and glycine are frequent
46
B-turn is stabilized by
HB between 1st aa: proline and 4th aa: glycine
47
What compacts a globular protein
B-turn
48
In polypeptides, 50% of the chain is : The other 50% is:
a-helix, B-turn (2*) Loops, coils (2*)
49
Non repetitive 2* structures include
Loops and coils
50
Formed by grouping of >2 types of 2* structures
motif or super 2*structure
51
examples of where motif or super 2* structure are present in
TF, DNA binding proteins, transmembrane proteins
52
Identify the following structures: Loop- helix- loop a-helix - B-turn - loop
motif or super 2* structure
53
Na-channel has __motifs each having__ connected with loops
4 six α-helices
54
Folding of 2* structures
3*
55
T/f: 3* structure retains all 2* structures
T
56
Forms a compact, globular or fibrous protein
3*
57
Hydrophobic aa residues are buried inside and Hydrophilic aa residues are found on the surface
3*
58
contain various domains
3*
59
functional parts of a 3o structure
Domains
60
Example of domains
Ca-binding domain ATP binding domain
61
Which part of 3* performs biological function
Domain
62
What are the Forces stabilizing a tertiary structure?
R groups H-bonding • Disulfide (-S-S-) bond • Ionic bonding • Hydrophobic interactions
63
Tendency of hydrophobic aa residues in a polypeptide to hide away from the aqueous environment is called as
hydrophobic interaction
64
Structure formed by association of more than one polypeptide
4*
65
T/f: 4* retains all 2* and 3* structures
T
66
4* is stabilized by
Non-covalent interactions between R groups
67
Disruption of all noncovalent interactions including 2o, 3o structures
Denaturation
68
Denaturation Disturbs which type of bonds
Noncovalent
69
Protein denaturation disrupts which structures
Secondary and tertiary
70
Give four examples of denaturant
PH, heat, urea and organic solvents
71
Denaturant do not disturb which type of bonds
Covalent bonds, such as peptide bonds di-sulfide
72
Addition of an amino acid gives rise to which disease
Huntington (gln
73
Deletion of an amino acid gives rise to which disease
Cystic fibrosis phe
74
Substitution of amino acids give rise to which disease
Sickle cell anemia glu—>val
75
Spontaneous changes in proteins structures give rise to which disease
Amyloidosis, prion diseases
76
Proline and lysine are frequent in
B-turns

Biochemistry (9 decks)

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