Lecture 4 Flashcards Preview

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Flashcards in Lecture 4 Deck (36):
1

peptide bond has a partial blank

double bond

2

peptide double bond restricts blank

rotation

3

blank amino acids are involved in catalysis

very few

4

rotation angle around Ca-N bond

phi

5

rotation angle around Ca-C bond

Psi

6

secondary structures

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

7

alpha helix is a blank handed corkscrew

right

8

alpha helix has hydrogen bonding between blank protons and blank oxygens

amide, carbonyl

9

keratin secondary structure is usually a blank

alpha helix

10

two aa that interrupt alpha helices

proline, glycine

11

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

flexible

12

why proline interrupts alpha helices

creates a kink because it's bent

13

beta sheet has a blank angle

extended

14

alpha helix has a blank angle

compact

15

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

beta sheet

16

beta sheets can be blank or blank in directions

parallel, antiparallel

17

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

antiparallel, stable

18

antiparallel beta sheets usually have a blank

beta turn

19

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

small, bent

20

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

globular

21

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

specific

22

blank folding is stabilized by interaction between side chains

long range

23

different stabilizing forces for tertiary structure

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

24

quaternary structure is stabilized by blank forces

similar to tertiary

25

hemoglobin has blank structure

multiple subunit

26

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

motifs

27

motifs suggest blank function

common

28

discrete, independently fodled, compact unit present in protein

domain

29

a single domain may have blank

multiple functions

30

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

denaturation

31

denaturation does not affect this structure

primary

32

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

chaotropic

33

folding is local and driven by the tendency to decrease blank

free energy

34

gibbs free energy is defined as

T = absolute temp
H = enthalpy
S = entropy

35

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

deltaG = deltaH - TdeltaS

36

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

primary structure