Lecture 4

Question 1

peptide bond has a partial blank

Answer 1

double bond

Question 2

peptide double bond restricts blank

Answer 2

rotation

Question 3

blank amino acids are involved in catalysis

Answer 3

very few

Question 4

rotation angle around Ca-N bond

Answer 4

phi

Question 5

rotation angle around Ca-C bond

Answer 5

Psi

Question 6

secondary structures

Answer 6

alpha helix, beta sheet, beta turn, loop (unstructured)

Question 7

alpha helix is a blank handed corkscrew

Answer 7

right

Question 8

alpha helix has hydrogen bonding between blank protons and blank oxygens

Answer 8

amide, carbonyl

Question 9

keratin secondary structure is usually a blank

Answer 9

alpha helix

Question 10

two aa that interrupt alpha helices

Answer 10

proline, glycine

Question 11

glycine is too blank which will not allow it to be in alpha helix

Answer 11

flexible

Question 12

why proline interrupts alpha helices

Answer 12

creates a kink because it’s bent

Question 13

beta sheet has a blank angle

Answer 13

extended

Question 14

alpha helix has a blank angle

Answer 14

compact

Question 15

secondary structure formed between linear regions of polypeptide chains. they are almost fully extended structures

Answer 15

beta sheet

Question 16

beta sheets can be blank or blank in directions

Answer 16

parallel, antiparallel

Question 17

sheets comprising blank chains are more blank than sheets of parallel sheets

Answer 17

antiparallel, stable

Question 18

antiparallel beta sheets usually have a blank

Answer 18

beta turn

Question 19

proline and glycine are good at making beta turns because glycine is blank and proline is blank

Answer 19

small, bent

Question 20

secondary structure elements in blank proteins fold relative to each other to make tertiary structure

Answer 20

globular

Question 21

tertiary structure of globular proteins is blank and is essential for correct biologic function

Answer 21

specific

Question 22

blank folding is stabilized by interaction between side chains

Answer 22

long range

Question 23

different stabilizing forces for tertiary structure

Answer 23

hydrogen, electrostatic interactions, van der waals interactions, hydrophobic effect, disulfide bonds

Question 24

quaternary structure is stabilized by blank forces

Answer 24

similar to tertiary

Question 25

hemoglobin has blank structure

Answer 25

multiple subunit

Question 26

recognizable combinations of secondary structure that appear in a number of different proteins

Answer 26

motifs

Question 27

motifs suggest blank function

Answer 27

common

Question 28

discrete, independently fodled, compact unit present in protein

Answer 28

domain

Question 29

a single domain may have blank

Answer 29

multiple functions

Question 30

this destroys secondary and tertiary structure of proteins by interfering with electrostatic interactions

Answer 30

denaturation

Question 31

denaturation does not affect this structure

Answer 31

primary

Question 32

the property of certain substances to disrupt the structure of water and thereby promote the solubility of nonpolar substances in water

Answer 32

chaotropic

Question 33

folding is local and driven by the tendency to decrease blank

Answer 33

free energy

Question 34

gibbs free energy is defined as

Answer 34

T = absolute temp
H = enthalpy 
S = entropy

Question 35

free energy change for a reaction at constant temp and pressure equation

Answer 35

deltaG = deltaH - TdeltaS

Question 36

knowing genetic code and the start codon and exon boundaries are known, it is possible to deduce the blank

Answer 36

primary structure