Ch 3/ Protein Structure and Function

Question 1

Non polar ameno acids letters

Answer 1

(London & Canada (C for cys)

Question 2

Uncharged polar ameno acid letters

Answer 2

NQSTY

Quit The Nozzey Shit You

Question 3

Basic ameno acid letters

Answer 3

(positve)

RKH

Kyle Rests Heavaly

Question 4

acidic ameno acid letters

Answer 4

Negative

DE

Dead Earth

Question 5

unique properties of water

Answer 5

given by H bonds

are thermal regulation and universal solvent

Question 6

Disolves in water

Answer 6

ionic and polar

Question 7

hydration shells

Answer 7

keeps ions seperage (also polar molecules), partal charge on O of water is attracted to ions making the schell

Question 8

hydrophobic effect

Answer 8

nonpolar subsances excluded from solvation netwoek of water

hydrophobic results in few water milecules on scheel, therefore released and spontatious

nonpolar has an orderd water chage, unfavered

Question 9

high number of hydrocarbons

Answer 9

non polar

Question 10

protines add

Answer 10

functionality

Question 11

functions of protines

Answer 11

structural, movement, defence, regulation, transport, catalusis

SM(all)

D(i)R(t)

T(i)K

Question 12

each protine folds into a

Answer 12

stable conformatin

Question 13

parts of ameno acid

Answer 13

Question 14

Unchared polar

Answer 14

capable of forming H bonds

H & OH-

Question 15

Nature prefers on __ over another

Answer 15

issomer

L ameno acids

D suggars

same with enzimes

Question 16

chiral

Answer 16

4 differnt groups

Question 17

Thalimonide

Answer 17

was racemic mixtre one form sedative other caused brith defects

not even just give one enantomer - because boddy convers it tothe other

Question 18

___ site on enzimes (are chiral)

Answer 18

allosteric site

Question 19

Peptide bond

Answer 19

covalent bond

connects two amino acids

amide linkage

e- is delocalized - exists as resonance

Question 20

formation of peptide bond

Answer 20

Question 21

type of reaction of peptide bond

Answer 21

condensation, dehydration,

Nuc. Acytl sub.

Question 22

How peptide bond affects protine conformation

Answer 22

rigid and planer

partial double bond charatar (b/c resonance)

not rotate freely (1/3 of bonds in peptide backbone)

limits conformation possibilites of protines

Question 23

Primary

Answer 23

linear ameno acid sequence

Question 24

secondary

Answer 24

basic folding units (helices, sheets)

Common patterns

Question 25

tertiary

Answer 25

3D structre of a folded prien (final)

Question 26

Quaternary

Answer 26

contains more than one polypeptide chain

Question 27

Priamary structure is listed from __ to \_\_

Answer 27

N (amino) terminous to C (carboxyl) terminous

Question 28

the backbone of the polpeptide excludes \_\_ is a repeating \_\_

Answer 28

r chains repeating CCN

Question 29

3D structure is determined by the

Answer 29

order of amino acids

Question 30

alfa heliex Bondong: R group: philic:

Answer 30

hydrogen bonding between N-H and c=O groups in polypeptide backbone (every 4 amino acids) Rgroup away from helix one side is hydropobic other side is hydrifilic (amphipathic)

Question 31

coiled coil

Answer 31

supper seoncdary alpha helies wrap around each other to form a stable sturctre two amphipathic come together (phobic binds w phobic phillic binds with phillic)

Question 32

Betta sheet

Answer 32

when polpeptide chain segments line up side by side each Betta sheet is fully extended and **stabalized by H bonding between N-h and carboxl groups WITHIN the polypeptide backbone** also amphipathic - goes above and below the plane, the R groups alternate up and down

Question 33

spider silk

Answer 33

stronger than steel

Question 34

pick sequenct that could fom a strand in a amphipathic beta sheet

Answer 34

alternating polar and nonpolar ameno acids

Question 35

tertiart structre

Answer 35

interacts of side chains/r groups

Question 36

Protine domains

Answer 36

substucture fold independantly into a stable compact structre each doman is a specific function of the protien (and structure)

Question 37

Globular protiens

Answer 37

soluable in H2O, compact structre, synamic function

Question 38

Fibrous protines

Answer 38

structural protines, long rod shape, insoluable in water

Question 39

Non covalent interactions include

Answer 39

vander wals H bonding electrostatic attractions

Question 40

vander wals

Answer 40

weak fromed with in close range between non polar atoms fluctuate electtral charges in close proximity

Question 41

H bonding

Answer 41

between hydrogen attom and small highly electroneg attom

Question 42

electrostatic attrations

Answer 42

salt bridges attration between ionic groups of opposite charges (ex. ionic bonds between acid and basic)

Question 43

Disulfide bridge/bond

Answer 43

forms when two cysteine residues are oxidized SH SH to S S

Question 44

Hemoglobin quaternary structure

Answer 44

2 alfa 2 beta chains each has a **heme** group that binds to oxygen (like a "pocket") 2 dimers slide past each other

Question 45

indivdual subunits of multimeric complexts ___ associate to from a \_\_

Answer 45

non-covalentaly (alows functionality because break and form eaisly) a functional protine structure

Question 46

problem of protine folding

Answer 46

cannot go though all possible conformations protines take less than a second to fold inside cell or in test tube

Question 47

Levinthal's paradox

Answer 47

astronomcal numbers of conformations open to a protine in a denatured state

Question 48

molten globule

Answer 48

protein states that are more or less compact, but are lacking the specific tight packing of amino acid residues which creates the solid state-like tertiary structure of completely folded proteins. formation of tertiary strutures but not fully there

Question 49

Native proteins

Answer 49

lowest energy form/ bottem of energy landscape model

Question 50

intermediates of energy landscape model

Answer 50

are more stable

Question 51

the folding code

Answer 51

themodynamic question of folding causes less disorder but it is spontanous (inc disorder in universe) how

Question 52

protine structure prediction

Answer 52

predit proteins native structre froma ameno acids

Question 53

the folding process

Answer 53

kientics a lof of possible pathways, how does it know which to take

Question 54

glibular proteins are __ proteins

Answer 54

soluble

Question 55

hydrophobic groups together in aquesous enviorment

Answer 55

hydrophobic groups togerher, water gets released into surroundsings (from water schell), increasing disorder

Question 56

Minimizing the nonpolar surface area (bury nonpolar groups in interior of folded protein) minimizes the

Answer 56

number of water molecules that become ordered water is freed, no longer organized aeound polpeptide

Question 57

denaturing of albumin in egg goes from

Answer 57

soluable to insoluable

Question 58

denaturing conditions

Answer 58

heat reducing agents detergents high salt mechanical stress

Question 59

heat

Answer 59

disrups weak bonds such as H

Question 60

Reducing agents

Answer 60

disulfide brige (covalant bond) is produced durring oxidation and removed with reduction

Question 61

detergents

Answer 61

get more on thiss amphipathic - hydrophobic and hydrophilic

Question 62

high salts

Answer 62

distrupt ionic bonds

Question 63

mechanical stress

Answer 63

ex. whisk egg white causes foam (with denatured protines)

Question 64

ligand

Answer 64

substance bound by the protine

Question 65

Indicate level(s) of protein structure to which each of the following contributes: a. hydrogen bond b. beta pleated sheet c. disulfide bond d. amino acid sequence

Answer 65

a. secondary, tertiary (quantanry if accaplable) b. secodary c. tertairy (quant if apiciable) d primary

Question 66

disulfide bond is caused by

Answer 66

teo cistines reducing