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Biochemistry > Amino acids (lectures 2&3) > Flashcards

Amino acids (lectures 2&3) Flashcards

1
Q

Ala

A

alanine

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2
Q

Arg

A

arginine

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3
Q

Asn

A

asparagine

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4
Q

Asp

A

aspartic acid

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5
Q

Cys

A

cysteine

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6
Q

Glu

A

glutamic acid

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7
Q

Gln

A

glutamine

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8
Q

Gly

A

glycine

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9
Q

His

A

histadine

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10
Q

Ile

A

isoleucine

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11
Q

Leu

A

leucine

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12
Q

Lys

A

lysine

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13
Q

Met

A

methionine

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14
Q

Phe

A

phenylalanine

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15
Q

Pro

A

proline

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16
Q

Ser

A

serine

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17
Q

Thr

A

threonine

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18
Q

Try

A

tryptophan

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19
Q

Tyr

A

tyrosine

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20
Q

Val

A

valine

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21
Q

A

A

alanine

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22
Q

R

A

arginine

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23
Q

N

A

asparagine

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24
Q

D

A

aspartic acid

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25
Q

C

26
Q

E

A

glutamic acid

27
Q

Q

28
Q

G

29
Q

H

30
Q

I

A

isoleucine

31
Q

L

32
Q

K

33
Q

M

A

methionine

34
Q

F

A

phenylalanine

35
Q

P

36
Q

S

37
Q

T

38
Q

W

A

tryptophan

39
Q

Y

40
Q

V

41
Q

aromatic R groups

A

phenylalanine
tyrosine
tryptophan

42
Q

positively charged R groups

A

lysine
arginine
histidine

43
Q

negatively charged R groups

A

aspartate

glutamate

44
Q

non polar, aliphatic R groups

A 
glycine 
alanine 
valine 
leucine 
methionine 
isoleucine
45
Q

polar, uncharged R groups

A 
serine 
threonine 
cysteine 
proline 
asparagine 
glutamine
46
Q

what are the side chains of negatively charged amino acids called?

A

carboxylates

COO- + H+

47
Q

what are the side chains of positively charged amino acids called?

A

primary amino groups

NH3+

48
Q

whats special about glycine?

A

has 2 hydrogens attached to an alpha carbon
has no D & L form
is found in flexible regions of the protein since its small side chain
it is a neurotransmitter

49
Q

whats special about cysteine?

A

has a thiol group (SH)
like hydroxyl but H is lost more easily
can bond to other cysteine by a disulphide bond
binds to metals in proteins

50
Q

when do proteins use disulphide bonds?

A

to increase their stability when working outside the cell

51
Q

whats special about histadine?

A

acts as a base - accepts a H+ below neutral pH
not strongly charged in the human body
can bind metals

52
Q

whats special about aromatic amino acids?

A 
are the largest 
hydrophobic 
found in the core of the protein 
absorb light & used in spectroscopy 
essential in the human diet
53
Q

what is phenylketonuria?

A

the inability to breakdown excess phenylalanine

54
Q

structure of amino acids

A

have complementary ends that fit together
each amino acid has a C & an N terminus
order determines protein character
is a zwitterion - no net charge
form stereoisomers & optical isomers
only L form found in proteins

55
Q

how are amino acids joined?

A

peptide bonds
condensation reaction
a covalent bond
peptide bond is rigid as it has a partial double bond character

56
Q

primary structure

A

linear sequence of amino acids joined by peptide bonds

57
Q

what is chloramphenicol?

A

an antibiotic used to treat eye infections & penicillin resistant meningitis
part of it looks like a peptide bond
binds to the bacterial ribosome where peptide bonds are made & kills the bacteria

58
Q

secondary structure

A

stabilised by H bonds
alpha helix
beta pleated sheet

59
Q

the alpha helix

A

not made by DNA
H bonds are made from the carbonyl oxygen on residue N to the amide nitrogen on residue N+4
has 3.6 residues per turn
successive side chains point outwards 100 degrees apart

60
Q

the beta sheet

A 
not made by DNA 
hydrogen bonds are between strands 
all side chains point alternatively up & down 
2 residue repeat 
forms sheets
61
Q

whats the different between antiparallel & parallel beta sheets?

A

antiparallel have straight H bonds so are a lot stronger

parallel are weaker as H bonds have a kink so less stable

Biochemistry (16 decks)

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