Lecture 3

Question 1

packing of secondary structural elements

Answer 1

tertiary structure

Question 2

organization of two or more polypeptide chains within a multisubunit protein

Answer 2

quaternary structure

Question 3

regularities in local conformations maintained by hydrogen bonds

Answer 3

secondary structures

Question 4

not all proteins have blank structure

Answer 4

quaternary

Question 5

protein folding occurs blank

Answer 5

quickly (10^-6 seconds)

Question 6

errors in protein folding can lead to things like this

Answer 6

alzheimers, cystic fibrosis, mad cow

Question 7

blank modification can influence folding

Answer 7

posttranslational

Question 8

protein folding helpers

Answer 8

chaperonins

Question 9

blank can interfere with folding

Answer 9

temperature

Question 10

change in dna sequence; amino acid substitution

Answer 10

mutations

Question 11

the protein must be blank in order to determine the primary structure

Answer 11

purified

Question 12

amino acid sequence; polymeric chain formed by covalently linked amino acids

Answer 12

primary structure

Question 13

R group influences the amount of blank

Answer 13

Flexibility

Question 14

Proline has a blank group instead of amino

Answer 14

Imino

Question 15

The amino acid proline differs from the other 19
amino acids because its sidechain is attached to the alpha amino group, NOT the alpha carbon.
T or F

Answer 15

False

Question 16

henderson hasselbeck blank goes on top

Answer 16

base

Question 17

trypsin cuts after blank or blank

Answer 17

lysine, arginine

Question 18

chymotrypsin cuts after

Answer 18

Phe, Tyr, Trp

Question 19

chymotrypsin and trypsin need help from blank

Answer 19

serine

Question 20

each peptide has a free blank

Answer 20

N-terminus

Question 21

peptide purification removes one blank at a time

Answer 21

amino acid