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Cell Biology > Ch 3/ Protein Structure and Function > Flashcards

Ch 3/ Protein Structure and Function Flashcards

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1
Q

Non polar ameno acids letters

A

(London & Canada (C for cys)

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2
Q

Uncharged polar ameno acid letters

A

NQSTY

Quit The Nozzey Shit You

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3
Q

Basic ameno acid letters

A

(positve)

RKH

Kyle Rests Heavaly

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4
Q

acidic ameno acid letters

A

Negative

DE

Dead Earth

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5
Q

unique properties of water

A

given by H bonds

are thermal regulation and universal solvent

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6
Q

Disolves in water

A

ionic and polar

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7
Q

hydration shells

A

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

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8
Q

hydrophobic effect

A

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

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9
Q

high number of hydrocarbons

A

non polar

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10
Q

protines add

A

functionality

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11
Q

functions of protines

A

structural, movement, defence, regulation, transport, catalusis

SM(all)

D(i)R(t)

T(i)K

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12
Q

each protine folds into a

A

stable conformatin

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13
Q

parts of ameno acid

A
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14
Q

Unchared polar

A

capable of forming H bonds

H & OH-

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15
Q

Nature prefers on __ over another

A

issomer

L ameno acids

D suggars

same with enzimes

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16
Q

chiral

A

4 differnt groups

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17
Q

Thalimonide

A

was racemic mixtre one form sedative other caused brith defects

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

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18
Q

___ site on enzimes (are chiral)

A

allosteric site

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19
Q

Peptide bond

A

covalent bond

connects two amino acids

amide linkage

e- is delocalized - exists as resonance

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20
Q

formation of peptide bond

A
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21
Q

type of reaction of peptide bond

A

condensation, dehydration,

Nuc. Acytl sub.

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22
Q

How peptide bond affects protine conformation

A

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

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23
Q

Primary

A

linear ameno acid sequence

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24
Q

secondary

A

basic folding units (helices, sheets)

Common patterns

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25
Q

tertiary

A

3D structre of a folded prien (final)

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26
Q

Quaternary

A

contains more than one polypeptide chain

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27
Q

Priamary structure is listed from __ to __

A

N (amino) terminous to C (carboxyl) terminous

28
Q

the backbone of the polpeptide excludes __

is a repeating __

A

r chains

repeating CCN

29
Q

3D structure is determined by the

A

order of amino acids

30
Q

alfa heliex Bondong:

R group:

philic:

A

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)

31
Q

coiled coil

A

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)

32
Q

Betta sheet

A

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

33
Q

spider silk

A

stronger than steel

34
Q

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

A

alternating polar and nonpolar ameno acids

35
Q

tertiart structre

A

interacts of side chains/r groups

36
Q

Protine domains

A

substucture

fold independantly into a stable compact structre

each doman is a specific function of the protien (and structure)

37
Q

Globular protiens

A

soluable in H2O, compact structre, synamic function

38
Q

Fibrous protines

A

structural protines, long rod shape, insoluable in water

39
Q

Non covalent interactions include

A

vander wals

H bonding

electrostatic attractions

40
Q

vander wals

A

weak fromed with in close range between non polar atoms

fluctuate electtral charges in close proximity

41
Q

H bonding

A

between hydrogen attom and small highly electroneg attom

42
Q

electrostatic attrations

A

salt bridges

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

43
Q

Disulfide bridge/bond

A

forms when two cysteine residues are oxidized

SH SH to S S

44
Q

Hemoglobin quaternary structure

A

2 alfa 2 beta chains

each has a heme group that binds to oxygen (like a “pocket”)

2 dimers slide past each other

45
Q

indivdual subunits of multimeric complexts ___ associate to from a __

A

non-covalentaly (alows functionality because break and form eaisly)

a functional protine structure

46
Q

problem of protine folding

A

cannot go though all possible conformations

protines take less than a second to fold inside cell or in test tube

47
Q

Levinthal’s paradox

A

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

48
Q

molten globule

A

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

49
Q

Native proteins

A

lowest energy form/ bottem of energy landscape model

50
Q

intermediates of energy landscape model

A

are more stable

51
Q

the folding code

A

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

52
Q

protine structure prediction

A

predit proteins native structre froma ameno acids

53
Q

the folding process

A

kientics

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

54
Q

glibular proteins are __ proteins

A

soluble

55
Q

hydrophobic groups together in aquesous enviorment

A

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

56
Q

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

A

number of water molecules that become
ordered

water is freed, no longer organized aeound polpeptide

57
Q

denaturing of albumin in egg goes from

A

soluable to insoluable

58
Q

denaturing conditions

A

heat

reducing agents

detergents

high salt

mechanical stress

59
Q

heat

A

disrups weak bonds such as H

60
Q

Reducing agents

A

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

61
Q

detergents

A

get more on thiss

amphipathic - hydrophobic and hydrophilic

62
Q

high salts

A

distrupt ionic bonds

63
Q

mechanical stress

A

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

64
Q

ligand

A

substance bound by the protine

65
Q

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

A

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

d primary

66
Q

disulfide bond is caused by

A

teo cistines reducing

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