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FM1010 > BIOCHEM - amino acids > Flashcards

BIOCHEM - amino acids Flashcards

1
Q

what is luciferase?

A

an enzyme that catalyses the production fo light from protein luciferin and ATP in fireflies

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2
Q

what are essential amino acids?

A

amino acids which cant be syntesised by the body

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3
Q

how many essentail aa’s are there?

A

9

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4
Q

draw general structure of an amino acid

A
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5
Q

what is the carbon at the centre of the aa called?

A

alpha carbon (Ca)

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6
Q

what s a steroisomer?

A
  • Isomers are molecules which have the same
    chemical formula but different chemical structures.
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7
Q

what is an enantiomer?

A

stereoisomers which are
mirror images of each other but cannot be
superimposed on each other.

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8
Q

what is the main type of amino acid in humans, L or D?

A

L

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9
Q

where are d amino acids found?

A

in peptides of
bacterial cell walls and
certain antibiotics

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10
Q

what are the classes of amino acids?

A
  1. Non-polar, aliphatic R groups
  2. Aromatic R groups
  3. Polar, uncharged R groups
  4. Positively charged R groups
  5. Negatively charged R groups
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11
Q

how are amino acids classified?

A

based on their
side chains (R groups)

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12
Q

properties of nonpolar, aliphatic r groups

A
  • Aliphatic R groups have linear chains of carbon atoms.
  • Do not accept or donate H+ ions.
  • Do not form hydrogen or ionic bonds.
  • They are hydrophobic
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13
Q

mnemonic for non polar, aliphatic amino acids? + what are they

A

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isoleucine
leucine
glycine
alanine
proline
valine
methionine

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14
Q

what is significant about proline?

A

it is an imino acid (not amino)

it has a ring structure which makes the proteins containing it very rigid, non flexible - collagen

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15
Q

what are the aromatic amino acids?

A

WYF
tryptophan , tyrosine, phenylalanine

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16
Q

why can proteins which contain aromatic aa’s absorb light? what frequncy can they absorb?

A

tryptohpan and tyrosine absorb UV light at 280 nm

17
Q

why are tyrosine and tryptophan more polar than phenylalanine

A

tryptophan - has an N indole ring

tyrosine - has an OH group

18
Q

whihc of the aromatic aa’s is least polar?

A

phenylalanine

19
Q

what are the polar, uncharged amino acids?

A

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serine, threonine, cysteine, asparagine, glutamine

20
Q

what modifications can be made to polar, uncharged aa’s?

A
  • Serine and threonine can be phosphorylated at their hydroxyl (OH) group.
  • Asparagine can have an oligosaccharide group attach to its amide group (N-glycosylation).
  • Serine and threonine can have an oligosaccharide group attach to their oxygen
    atom (O-glycosylation).
21
Q

what is significant about the bonding properties of cysteine?

A

sulfhydryl group - can from disulphide bonds

important for protein structure

strongly hydrophobic

22
Q

what are the positively charged AA’s?

A

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arginine, lysine, histidine

23
Q

why is histidine weakly basic?

A

imidazole ring

24
Q

do positively charged R groups have acidic or basic side chains?

A

basic

25
Q

do negatively charged R groups have acidic or basic side chains?

A

acidic

26
Q

what are the acidic AA’s?

A

glutamiae, aspartate

27
Q

what are uncommon amino acids?

A

amino acids that have been modified from common amino acids after they have been incorporated into a polypeptide.

28
Q

give examples of uncommon amino acids. where are these found?

A

4-hydroxyproline and 5-hydroxylysine
collagen

creatine
in cells, used as an alternative energy source

29
Q

are all uncommon amino acids found in proteins?

A

no. creatine in skeletal muscle

ADP + phsophocreatine ->ATP + creatine

30
Q

how are amino acids linked to form proteins?

A

peptide bonds

31
Q

how are peptide bonds fomred?

A

condensation of the alpha carboxyl of one amino acid with the alpha-amino of another

FM1010 (11 decks)

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