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BCM > BCM9 > Flashcards

BCM9 Flashcards

1
Q

What is the Pka of the amino group?

A

9.6

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2
Q

What is the Pka of the carboxyl group?

A

2.2

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3
Q

What are AA referred to as?

A

amphoteric

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4
Q

What is the isoelectric point?

A

pH at which protein has no over all charge

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5
Q

What does a high pKa mean?

A

it is less likley to dissociate

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6
Q

What is the rule for determining if an AA is charged?

A

if Narg + Nlys > Nasp + Nglu

= charged at neutral pH and pka > 7

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7
Q

What is the corn law?

A
  • put h behind carbon
    CO - R - N
    if clockwise it is the l form
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8
Q

Where are D amino acids found?

A

peptidoglycan

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9
Q

What are the amino acids with a postively charged side chain at neutral ph?

A

arginine
lysine
- histinde = partially positive

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10
Q

what are the amino acids with a negatively charged side chain at neutral ph?

A

aspartic acid

glumatic acid

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11
Q

pka of aspartic acid?

A

4.1

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12
Q

pka of glutamic acid?

A

4.1

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13
Q

pka of histine

A

6.1

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14
Q

pka of argine

A

12.5

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15
Q

pka of lysine

A

10.8

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16
Q

why is histine only partially charged at ph7?

A

as imidazole ring loses proton above ph6..1

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17
Q

what is the guanidium group?

A

NHC(NH2)2

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18
Q

where is a guanidium group found?

A

arigine

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19
Q

What is found on the side chain of glutamic acid?

A

carboxylate group

which is stabilised by resonance

20
Q

how is guanidium group stabilised?

A

resonance

21
Q

What are the 5 amino acids with polar uncharged side chains

A

asparagine
threonine
serine
glutamine

22
Q

what ate the 8 amino acids with hydrophobic side chains?

A 
alanine
phenyl alanine
leucine
isoleucine 
valine
methionine
tyrosine
tryptophan
23
Q

what are the 3 amino acids containing aromatic rings?

A

phenylalanine
tyrosine
tryptophan

24
Q

what do not form in the cytosol?

A

disulfide bonds

25
Q

what are disulfide bonds used for?

A

help rigidity where proteins would become unorganised

eg. outside of cell in changing pH or temp

26
Q

what do disulfide bonds form between?

A

two cysteine residues

27
Q

what is a peptide bond?

A

-CONH

28
Q

where does the equilbrium lie to in peptide bond formation?

A

the left

29
Q

what catalyses peptide bond formation?

A

ribosome

30
Q

what cataylses peptide bond hydrolysis?

A

proteases or proteinases

eg. trypsin, chymotrypsin, collagenase

31
Q

draw and name the mechanism that occurs in peptide bond formation?

A

addition elimination

  • nucleophillic attach of carbony by lone pair of electrion from amino group
  • results in h20 elimination
32
Q

what is the reality of peptide bond formation mechanism?

A

both carboylate ion and amino group will be charged
extra proton on amino group transfered to carboxylate during the reaction
the o- acts as a nucelophile on one of the hydrogens

33
Q

what defines a condensation reaction?

A

water eliminated

- protein residues = lack water

34
Q

what is the peptide bond?

- draw structures

A

a resonance hybrid structure between two competeting structures = double bond character
delocalisation of pi electron over entire peptide boind rather than simply over the c=o bond
-

35
Q

why is NHCO bond planar?

A

restricted rotation around around NH-CO bond

due to double bond characteristic of NH CO

36
Q

which conformation frorm is favoured in peptide bonds and by what amount?
why?
draw

A

trans 1000:1

or there could be steric clashes or r groups

37
Q

what conformation from is favoured in prolines?

and by what amount

A

trans 15:1

38
Q

what are 4 other AA acids found in the cell and where?

A

ornithine - urea cycle
citrulline - urea
selenocysteine - rare, few proteins
homocysteine - cysteine + extra ch2

39
Q

give examples of amino acid neurotransmitters

A

glutamate

GABA

40
Q

what does neurotransmitter gaba do?

A

inhibitory neurotransmitter

release opens cl- channels

41
Q

what does glutamate do?

A

release leads of opening of cation channels and depolarisation of the membrane

42
Q

What amino acids can be post translationally modified by phosphorylation?

A

serine
threonine
tyrosine
residues

43
Q

which amino acids can be glycosylated and where?

A 
serine
threonine
asparagine
side chains
in endoplasmic reticulum and golgi body
44
Q

what is the most common post translational modification?

A

acetylation of amino group and N terminal resudies

45
Q

give examples of 4 post translational modifications

A
  1. myristoylation - add lipid for membrane proteins
  2. ubiquinination and sumoylation and acetylation of lysine
  3. thrombin cleaves fibrogen to fibrin
  4. transglutaminase cross link lysine and glutamine

BCM (27 decks)

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