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UE1 Biochimie > Acides aminés > Flashcards

Acides aminés Flashcards

1
Q

speci glycine

A

pas de C asym

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2
Q

speci methionine

A

1 S au milieu chaine lateral

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3
Q

speci proline

A

chaine laterale liee au c et N de amine = formation d’un cycle

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4
Q

speci phenylalanine

A

cycle phenyl
aromatique
absorbe ds UV

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5
Q

speci tryptophane

A

groupe indol

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6
Q

aa phosphorisables

A

seurine
treonine
tyrosine

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7
Q

aa groupe phenyl

A

tyrosine

phenylalline

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8
Q

aa soufree thiol SH

A

cysteine

pont possible S-s

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9
Q

aa amide

A

asparagine (N glycolisation possible)

glutamine

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10
Q

aa q-

A

acide aspartique et glutamique

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11
Q

aa neutre

A

histidine (heterocycle)

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12
Q

aa q+

A

arginine

lysine (HAL)

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13
Q

structure prot

A

Ie : l peptidique aa, angle, rupture l pepti
IIe : reguliere/repe (a-b) OU irre/irre (coudes / boucles)
IIIe : repliement chaine aa : l faibles et covalentes
IVe : prot multimerique

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14
Q

carac l pepti 2 aa

A

polaire
plane
rigide
amide particuliere

N term (d) a C term (COOH)

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15
Q

angle omega

A

CIS = 0 ou TRANS = 180 (+ stable)

torsion autour C=0 et NH

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16
Q

angle phi

A

rotation C NH

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17
Q

angle psy

A

angle C C=O

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18
Q

carac communes phi et psy

A
  • deter organisaiton spatiale chaine polypetidque

- fixee pour struc II donnee

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19
Q

qui peut rupturer l peptique

A

enz protease

agent chimique bromure de cyanogene

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20
Q

l pep aaa chymotripsine

A

apres leucine, methioinine, trypto, tyro, phenyl (arom)

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21
Q

l pep aa tripsine

A

lysine, arginine (q+)

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22
Q

seules chaines laterales chargees

A

pH = 7
arginine, lysine (basique)

acide aspartique, acide glutamique

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23
Q

position chaine laterales des aa de helice alpha et feuillet beta

A
  • vers ext

- au dessus et en dessous feuillet

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24
Q

II repetition Lh

A
  • O donnuer, N acceptuer

- entre pls brins

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25
Q

carac feuillet

A

anti paral

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26
Q

motifs, domaines II

A

helice coude helice

immunoglobuline

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27
Q

def coudes vs boucles

A
  • qq aa residus (eg coude beta = 4 residus aa stabilises pas 1LH)
  • 20 aa
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28
Q

aa frequent helice alpha

A

alanine

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29
Q

aa frequent feuillet beta

A

valine

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30
Q

aa frequent coudes

A

glycine, proline

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31
Q

L faibles III

A
  • hydrogenes
  • ioniques
  • Van der Waals
    hydorphobes : mol apolaires : prot transmembranaire
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32
Q

III : l covalentes

A

pt disulfure

strcu I deter III

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33
Q

agent denaturant l faibles

A

SDS
uree M
chlorure de guanidium

34
Q

=> perte struc III

A

perte act

35
Q

def struc IV

A

asso pls sous unites via LH faibles ou ponts S2 INTER catenaires

36
Q

Methionine peut former un pont disulfure avec cysteine

A

Non

Mais residu de methio est coupee par bromure de cyanogene

37
Q

L pepti peut être coupée par bromure de cyanogen et ?

A

Oui

38
Q

Charge -

Quel aaa ds chromato

A

Acide = -

Donc attiree vers +

39
Q

L ioniques intervient majori ds stabilite helices alpha ?

A

Non LH, N donneur et O accepteur

40
Q

Phosphorisation des aaa alcools peut participer à la struc IV ou III des prot

A

Oui

41
Q

Tryptophane props chaine laterale

A

Un des constituants des segments transmembranaires des prots

42
Q

Aaa acec une CYS peut former points disulfure

A

Non ik faut plus que 1

43
Q

Lysine contient 2 fonctions NH3+ ?

A

Oui une sur c alpha et une sur chaine lat

44
Q

Histide caract

A

Chaine ionisable

Pka=6

45
Q

Si on coupe avec trypsine prot avec arginine, on obt cb de peptides

A

2

46
Q

chymotrypsine coupe

Asp-His-Glu-Leu-Val-Ser-Thr-Asn-Phe-Arg, a borne + et - quelles aa

A
  1. trouver coupes a quel niveau apres Leucine et Phe (pas thr)
    • asp donc possede histidne or histi faiblement basique
  3. neutre : un aa phosp puisque serine et theronine
47
Q

speci histidine

A

faiblement basique

48
Q

chymotrypsine : entre le tryptophane et l’acide aminé le précédant.

A

faux apres

49
Q

tryptophane : plutot quelle region interne/ext des prot

A

int car hydrophobe

50
Q

qui possede fonciton guanidium

A

arginine

51
Q

arginine sous forme protonee a ph=7

A

oui car basique

52
Q

glutamine quelles fonctions

A

amide et amine

53
Q

b aa apportes que par lalimentation

A

9

54
Q

qui absorbe FORTEMENT ds UV et pq

A

tous cycles ( phye - tyrosine - TRYP) - electrons pi delocalises

55
Q

quels aa peuvent ajouter un groupement phosphate

A

les aa phosphirable car OH

56
Q

q charge apporte phosphiraltion

A

charge negative

57
Q

ct formaiton pont disulfure

A

OXYDATION de foncitions thiols protes par 2 cysteine

58
Q

aa ramifie

A

valine leucine isoleucine

59
Q

acide glutamique pka et nombre de C

A

2 C puis COO- 4.1

60
Q

pka histine

A

6 - neutre a 7 - positive a 5 (moyen de regulation des enzymes)

61
Q

histine struc

A

heterocycle ( N et C) –> a un certain cract aromatique

62
Q

diff lysine vs arginine

A

primaire 10.5 / guanidium 12.5 et 2 N en plus ds chainec=NH3+ avant dernier NH2

63
Q

quel aa chaine lat = methyl

A

alanince`

64
Q

quels aa chaine lat ramifiee

A

valine leucine isoleucine`

65
Q

quel aa groupe indol

A

tryptophne

66
Q

quel aa prensece d;un cycle

A

proline (R=3C)

67
Q

quel aa est amide

A

glutamine (R=3C) et asparagine

68
Q

quel aa 2 cycles

A

indol —> trypto

69
Q

pka acide glutamnique

A

4.1

70
Q

pka acide asparti

A

3.9

71
Q

pka histidine

A

7

72
Q

pka lysine

A

10.5

73
Q

pka arginine

A

12.5

74
Q

a ph cb hisine chargee +

A

ph=5

75
Q

quel aa polaire a un cycle

A

hisrin

76
Q

quel aa polaire a un certain caract arom

A

histidine

77
Q

aa avec R = 4C + fonction speci

A

lysine leucine isoleucine LILa Lille on mange des crepes)

78
Q

aa avec R = 3C

A

valine metrhi prolien (cycle) VMP= vitesse moyenne de prout = maman

79
Q

aa ac R=2C

A

threosiine glutamine <3 AH glutamique = TG (noah says tagueule car tres mal eleve donc punit teere ss eau_

80
Q

aa avec R=1C

A

alanine serine tyrosine cysteine phenyanine asparagine <3 AH asparitique PS CATA = ps cafe de la catastiophe on rentre que avec cravate

81
Q

chymotrysine apres proline ou phenyla

A

pheny

82
Q

chymitryp apres tryptophane ou tyrosine

A

tyrosine

UE1 Biochimie (7 decks)

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