Chapter 4

Question 1

Beta sheet structure

Answer 1

Pleats

Question 2

Types of secondary structures

Answer 2

Alpha helix
Beta sheet
Beta turn
Left hand helix

Question 3

Primary structures

Answer 3

Sequence of amino acids shows all covalent bonds

Question 4

Weight of amino acid

Answer 4

110 D

Question 5

Alpha helixes are held together by

Answer 5

Hydrogen bonds

Question 6

Alpha helix HB relationship

Answer 6

i to I+4

Question 7

Supersecondary motif

Answer 7

Part of bigger structure

2 or more secondary structures

Question 8

Random coil region

Answer 8

Amino acid that does not adopt uniform secondary structure

Can still adopt structure just not secondary

Question 9

Where is right alpha helical region on ramachandran plot

Answer 9

Bottom left

Question 10

Salt bridges form between

Answer 10

Acidic and basic amino acids

Acidic and metal

Question 11

Hydrogen bonding for aa

Answer 11

Interactions between R group and

other R, backbone, water

Question 12

Covalent for as

Answer 12

Other amino acids cross linked
Cysteine
Isopeptide Lys Glu Asp

Question 13

Quaternary structure

Answer 13

3D structure of 2 or more polypeptides

Question 14

2 of the same polypeptides joined together are called

Answer 14

Homodimer

Question 15

Hemoglobin can be described as

Answer 15

Dimer of diners
Tetramer
Heteroligomer

Question 16

What are the 3 classes of tertiary class

Answer 16

All alpha helix
All beta sheet
Mixed

Question 17

What drives protein folding

Answer 17

Hydrophobic effect

Question 18

What are globular proteins

Answer 18

Spheral or elliptical
Enzymatic regular roles
Water soluble

Question 19

What is a fibrous protein

Answer 19

Long rod
Play structural and protective
Insoluble

Question 20

What is the first step of protein folding

Answer 20

Very fast
Simple secondary structure
Alpha helix
Beta hairpin

Question 21

2nd step of protein folding

Answer 21

Hydrophobic effect

Milton globule incomplete secondary structure

Question 22

3rd step of protein folding

Answer 22

Rearrangement

More water excluded

Question 23

What are characteristic of peptide bond

Answer 23

Partial double bond character prevents rotation
Rigid
Lack of rotation prevents other structures

Question 24

What is the bond that forms between cytesiene residues

Answer 24

Disulphide

Question 25

Why is primary structure important

Answer 25

Determines protein folding

Question 26

R groups of amino acids residues in alpha helix ___

Answer 26

Bristle out from axis of helix

Question 27

R groups on beta strand

Answer 27

Alternate one side and other

Question 28

Phi angle

Answer 28

Angie of rotation about the bond between N atom and alpha C

Question 29

Psi angle

Answer 29

Angle of rotation between alpha carbon and carbonyl carbon

Question 30

Beta strand

Answer 30

Fully extended polypeptide chain

Question 31

Domain

Answer 31

Compact region may be connected by flexible polypeptide chain

Question 32

Folding funnel

Answer 32

Energy landscape

Question 33

Molten globule

Answer 33

Structure characterized by dynamic hydrophobic interactions

Question 34

Metamorphic protein

Answer 34

Exist in an ensemble of structures of approximately equal energy in equilibrium

Question 35

Intrinsically disordered proteins __

Answer 35

That’s in whole or part lack discrete 3D structure under physiological conditions

Question 36

Prion

Answer 36

Cause of spongiform encephalopathies

Question 37

What stabilizes tertiary structure

Answer 37

HB Salt bridges Mainly van der waals

Question 38

What are the 3 steps of affinity purification

Answer 38

Column has Ni or Co Wash protein bound Elute

Question 39

Why does the pH have to be 8 for affinity purification

Answer 39

His must be neutral

Question 40

What is BME

Answer 40

Reducing agent breaks disulfide bonds

Question 41

What is DTT

Answer 41

Reducing agent breaks disulphide bonds

Question 42

How are disulphide bonds formed

Answer 42

Oxidation