Proteins and Amino Acids - 1 Flashcards

1
Q

what are proteins ?

A

linear unbranched chains of amino acids that are joined by peptide bonds ( CONH)

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2
Q

what occurs to the N and C termini at physiological pH (7.4)

A

They carry charges - the C terminus is negative and the N terminus is +

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3
Q

how many different kinds of amino acid residues is there and what determines this ?

A

the genetic code determines only 20 different amino acid residues.

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4
Q

how is a protein produced ?

A

By translation that occurs in the at the ribosme

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5
Q

how will the other residues be found ?

A

By post translational modification , i.e addition of hydroxyl group

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6
Q

what is the most common form of configuration D or L and how are they designated ?

A

chiral alpha carbon descides if D or L . L configuration is most common in natural proteins. D does occur must is rare and found in bacteria mostly.

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7
Q

single letter code G

A

glycine

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8
Q

v

A

valine

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9
Q

i

A

isoleucine

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10
Q

s

A

serine

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11
Q

c

A

cysteine

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12
Q

N

A

asparagine

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13
Q

w

A

tryptophan

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14
Q

m

A

methionine

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15
Q

a

A

alanine

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16
Q

l

A

leucine

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17
Q

p

A

proline

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18
Q

t

A

threonine

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19
Q

F

A

phenylalanine

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20
Q

Q

A

glutamine

21
Q

Y

A

tyrosine

22
Q

where they charged or uncharged ?

A

uncharged

23
Q

d

A

aspartic acid co2-

24
Q

k

A

lysine NH3+

25
Q

R

A

arginine NH3+

26
Q

E

A

glutamic acid C02-

27
Q

H

A

histidine NH+ ring

28
Q

are they charged or uncharged ?

A

charged

29
Q

what is a pKa value ?

A

it indicates the strength of an acid and how much it dissociates in water

30
Q

what does a low pKa value indicate

A

a strong acid as it will dissociate more fully in water.

31
Q

whats the 2 unusual amino acids and why ?

A

glycine - no side chain

proline - bends round on itself and is an imino as contains amine and carboxyl group

32
Q

if an OH is present in an amino acid what can form?

A

hydrogen bonds , stabilises

33
Q

if an SH present what can form ?

A

disulphide bridge , covalent and stabilises

34
Q

what is the primary structure of a protein ?

A

this is the linear chain of amino acids

35
Q

how come the amino acid sequence is subject to change ?

A

due to genetic mutations

36
Q

how come proteins evolve over time ?

A

due to the mutations that occur

37
Q

where is the information held to define the 3D structure of a protein?

A

in the primary sequence

38
Q

whats the stages of a secondary structure forming ?

A

The polypeptide chain will fold at certain points which then pack together to form a domain. These domains then dock.

39
Q

what do secondary structures originate from ?

A

stereochemical restrictions on the chain conformations

40
Q

what geometry does the peptide bond have and why?

A

planar due to the delocalisation of electrons across the C-N bond , therefore cannnot rotate

41
Q

What bonds can rotate in the peptide bond?

A

those either side of the alpha carbon

42
Q

are all combinations of phi and psi bonds energetically favourable ?

A

no as some have steric overlap of neighbouring atom especially if a side chain is present

43
Q

what’s the most energetically favourable angle ?

A

when the amide groups can form hydrogen bonds between them

44
Q

where is the hydrogen bonds in an alpha helix ?

A

in the amide backbone

45
Q

whats the orientation of the side chains in an alpha helix ?

A

they stick outwards

46
Q

what is a dipole and why is it present on the helix ?

A

this is a seperation in charge and due to the positive carbon and negative oxygen

47
Q

what protein is nearly all alpha helix ?

A

keratin

48
Q

what occurs to an alpha helix as it gets longer ?

A

it bends