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Biochemistry > L12 > Flashcards

L12 Flashcards

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
Q

How are 2* stabilized?

A

HB

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26
Q

One turn in a-helix structure contains

A

3.6 aa

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27
Q

Rise per aa in a-helix

A

1.5A*

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28
Q

Side chains in a helix are extended__
While in B-sheet __

A

outwards
Up, down

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29
Q

a-helix can be broken by heat and other denatures unlike __

A

Peptide bonds

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30
Q

Rare ?(a-helix a-helix3 pi-helix)

A

a-helix3 pi-helix)

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31
Q

Most relaxed (a-helix a-helix3 pi-helix)

A

a-helix3

32
Q

Most condensed (a-helix a-helix3 pi-helix)

A

pi-helix

33
Q

aa/ turn for (a-helix a-helix3 pi-helix)

A

3.6
3
4.4

34
Q

HB between which aa in (a-helix a-helix3 pi-helix)

A

1-4
1-3
1-5

35
Q

What are the aa that disrupts the a-helix

A

Proline: H❌
Glycine: too flexible

36
Q

Mention the % of a-helix in (keratin, myoglobin, chymotrypsin)

A

100%
80%
~0%

37
Q

Formed by bending of a polypeptide segment over another

A

B-sheet

38
Q

Surface appears pleated

A

B-pleated sheet

39
Q

B-sheet is stabilized by

A

HB

40
Q

Is ridged

A

B-structure

41
Q

Proline and glycine aa
are incompatible or disrupt this structure

A

B-sheet

42
Q

Formed by abrupt disruption of the β-sheet

A

B-turn

43
Q

Reverses the direction of β-sheet

A

β-turn

44
Q

Connects two successive B-sheets

A

B-turn

45
Q

How many aa is B-turn made up of

A

4aa, proline and glycine are frequent

46
Q

B-turn is stabilized by

A

HB between 1st aa: proline and 4th aa: glycine

47
Q

What compacts a globular protein

A

B-turn

48
Q

In polypeptides,
50% of the chain is :
The other 50% is:

A

a-helix, B-turn (2)
Loops, coils (2)

49
Q

Non repetitive 2* structures include

A

Loops and coils

50
Q

Formed by grouping of >2 types of 2* structures

A

motif or super 2*structure

51
Q

examples of where motif or super 2* structure are present in

A

TF, DNA binding proteins, transmembrane proteins

52
Q

Identify the following structures:
Loop- helix- loop
a-helix - B-turn - loop

A

motif or super 2* structure

53
Q

Na-channel has __motifs each having__ connected with loops

A

4

six α-helices

54
Q

Folding of 2* structures

A

3*

55
Q

T/f: 3* structure retains all 2* structures

A

T

56
Q

Forms a compact, globular or
fibrous protein

A

3*

57
Q

Hydrophobic aa residues are
buried inside and Hydrophilic aa residues are
found on the surface

A

3*

58
Q

contain various domains

A

3*

59
Q

functional parts of a 3o structure

A

Domains

60
Q

Example of domains

A

Ca-binding domain
ATP binding domain

61
Q

Which part of 3* performs biological function

A

Domain

62
Q

What are the Forces stabilizing a tertiary structure?

A

R groups
H-bonding
• Disulfide (-S-S-) bond
• Ionic bonding
• Hydrophobic interactions

63
Q

Tendency of hydrophobic aa residues in a polypeptide to hide away from the aqueous environment is called as

A

hydrophobic interaction

64
Q

Structure formed by association of more than one polypeptide

A

4*

65
Q

T/f: 4* retains all 2* and 3* structures

A

T

66
Q

4* is stabilized by

A

Non-covalent interactions between R groups

67
Q

Disruption of all noncovalent interactions including 2o, 3o structures

A

Denaturation

68
Q

Denaturation Disturbs which type of bonds

A

Noncovalent

69
Q

Protein denaturation disrupts which structures

A

Secondary and tertiary

70
Q

Give four examples of denaturant

A

PH, heat, urea and organic solvents

71
Q

Denaturant do not disturb which type of bonds

A

Covalent bonds, such as peptide bonds di-sulfide

72
Q

Addition of an amino acid gives rise to which disease

A

Huntington (gln

73
Q

Deletion of an amino acid gives rise to which disease

A

Cystic fibrosis phe

74
Q

Substitution of amino acids give rise to which disease

A

Sickle cell anemia glu—>val

75
Q

Spontaneous changes in proteins structures give rise to which disease

A

Amyloidosis, prion diseases

76
Q

Proline and lysine are frequent in

A

B-turns

Biochemistry (9 decks)

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