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BIOCHEM LEC > AMINO ACIDS (20) > Flashcards

AMINO ACIDS (20) Flashcards

1
Q
  • Aliphatic R group
  • nonpolar
  • non-essential
  • Hydrophobic
  • Ambivalent
  • Neutral
  • R group: Methyl group
A

ALANINE
[A]
Ala

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2
Q

ALIPHATIC AMINO ACIDS
they are also hydrophobic

A

VALINE
ISOLEUCINE
ALANINE
LEUCINE
GLYCINE

VIALG

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3
Q
  • Aliphatic R group
  • polar
  • essential
  • Basic
  • R group: Guanidino group
A

ARGININE
[R]
Arg

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4
Q
  • designed to BIND with PHOSPHATE
  • important in NITROGEN METABOLISM
A

ARGININE
[R]
Arg

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5
Q

Test / Reaction for ARGININE

A

SAKAGUCHI TEST

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6
Q

amino acids with GUANIDINO GROUP

A

HISTIDINE
ARGININE
LYSINE

History ng Argentina is a Ly (lie)

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7
Q
  • Aliphatic R group
  • polar
  • non essential
  • Acidic
  • R group: Carboxyl group
A

ASPARTIC ACID
[D]
Asp

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8
Q

one of the ACIDIC amino acid; acts as GENERAL ACIDS in ENZYME ACTIVE CENTERS

A

ASPARTIC ACID
[D]
Asp

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9
Q
  • Aliphatic R group
  • polar
  • non essential
  • R group: Amide group
A

ASPARAGINE
[N]
Asn

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10
Q
  • amide of aspartic acid
  • common site for attachment of CARBOHYDRATES IN GLYCOPROTEINS
A

ASPARAGINE
[N]
Asn

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11
Q

ACIDIC AMINO ACIDS

A

GLUTAMIC ACID
ASPARTIC ACID

GooD

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12
Q
  • Aliphatic R group
  • nonpolar
  • non essential
  • R group: Thiol group
A

CYSTEINE
[C]
Cys

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13
Q
  • plays a key role in STABILIZING EXTRACELLULAR PROTEINS
  • can react with ITSELF to form an oxidized dimer by formation of a DISULFIDE bond
A

CYSTEINE
[C]
Cys

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14
Q

SULFUR CONTAINING amino acids

A

CYSTEINE
METHIONINE

si ClassMate may Sulfur

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15
Q
  • Aliphatic R group
  • polar
  • non essential
  • R group: Carboxylic acid
A

GLUTAMIC ACID
[E]
Glu

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16
Q
  • has one additonal CH₃
  • interconvertible with α-ketoglutarate
  • important in the BIOSYNTHESIS OF PROLINE
A

GLUTAMIC ACID
[E]
Glu

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17
Q
  • Aliphatic R group
  • nonpolar
  • non essential
  • R group: Hydrogen atom
A

GLYCINE
[G]
Gly

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18
Q
  • SMALLEST amino acid
  • ambivalent
  • exists mainly as zwitterion
  • together with porline, favors the formation of beta-turn/bends
  • simplest
  • low molecular wieght
  • not chiral
A

GLYCINE
[G]
Gly

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19
Q
  • Aromatic R group
  • polar
  • essential
  • basic
  • R group: Imidazole
A

HISTIDINE
[H]
His

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20
Q
  • Aliphatic R group
  • nonpolar
  • essential
  • R group: methyl group (sec butyl)
A

ISOLEUCINE
[I]
Ile

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21
Q

side chain is NOT REACTIVE and therefore NOT INVOLVED in any COVALENT CHEMISTRY in enzyme active centers

A

ISOLEUCINE
[I]
Ile

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22
Q
  • Aliphatic R group
  • nonpolar
  • essential
  • R group: Isobutyl
A

LEUCINE
[L]
Leu

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23
Q
  • has one additional methylene group in its side chain compared with valine
  • hydrophobic; buried in folded proteins
A

LEUCINE
[L]
Leu

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24
Q
  • Aliphatic R group
  • polar
  • essential
  • POSITIVELY CHARGED ɛ-amino group
  • R group: amino group
A

LYSINE
[K]
Lys

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25
Q
  • Aliphatic R group
  • nonpolar
  • essential
  • R group: methylthioether
A

METHIONINE
[M]
Met

26
Q
  • has thiol ether
  • plays role in metabolism forming SAM which act as METHYL DONOR during METHYLATION
A

METHIONINE
[M]
Met

27
Q
  • Aromatic R group
  • nonpolar
  • essential
  • R group: Benzyl group
A

PHENYLALANINE
[F]
PhE

28
Q
  • derivative of alanine with a phenyl substituent on the β carbon
  • hydrophobic
A

PHENYLALANINE
[F]
Phe

29
Q
  • Aliphatic R group
  • nonpolar
  • non essential
  • R group: Pyrrol group
A

PROLINE
[P]
Pro

30
Q
  • an IMINO ACID
  • when found in an α helix, the helix will have a slight bend due to the lack of the hydrogen bond
  • found at the end of a helix or in turns or loops
A

PROLINE
[P]
Pro

31
Q
  • Aliphatic R group
  • polar
  • non essential
  • R group: Hydroxymethyl group
A

SERINE
[S]
Ser

32
Q
  • differs from alanine in that one of the methylenic hydrogens is replaced by a hydroxyl group
  • hydrophilic
A

SERINE
[S]
Ser

33
Q

OH conatining amino acids

A

SERINE [S]
THREONINE [T]
TYROSINE [Y]

STY

34
Q
  • Aliphatic R group
  • polar
  • essential
  • R group: hydroxyl group
A

THREONINE
[T]
Thr

35
Q
  • non aromatic OH
  • α and β carbons are optically active
A

THREONINE
[T]
Thr

36
Q

capable of rotating plane polarixed light either to the left or right

A

OPTICALLY ACTIVE

37
Q
  • Aromatic R group
  • nonpolar
  • essential
  • R group: Indole ring
A

TRYPTOPHAN
[W]
Trp

38
Q

amino acids with RING

A

HISTIDINE
TRYTOPHAN
TYROSINE
PHENYLALANINE

WHYP

39
Q
  • Aromatic R group
  • polar
  • nonessential
  • R group: Phenolic
A

TYROSINE
[Y]
Tyr

40
Q

is derived form phenylalanine by hydroxylation in the para position

A

TYROSINE
[Y]
Tyr

41
Q
  • Aliphatic R group
  • nonpolar
  • essential
  • R group: Isopropyl group
A

VALINE
[V]
Val

42
Q

hydrophobic, usually found in the interior of proteins

A

VALINE
[V]
Val

43
Q
  • does not bind or give off protons or participate in H or ionic bonds (alkyl groups, aromatic)
  • side chain can be thought as “oily” or lipid like
  • hydrophobic
A

NON POLAR AMINO ACIDS

44
Q
  • zero net charge at neutral pH
A

UNCHARGED POLAR amino acids

45
Q

these can lose proton at alkaline pH

A

CYSTEINE [C]
TYROSINE [Y]

46
Q

contain a polar OH- group that can participate in H-bond formation

A

SERINE [S]
THREONINE [T]
TYROSINE [Y]

47
Q

contain a C=O group and an amide grup (both can participate in H-bond formation)

A

ASPARAGINE [N]
GLUTAMIC ACID [E]

48
Q

POLAR amino acids should contain

A

Sulfur
Oxygen
Nitrogen

49
Q
  • proton donors
  • fully ionized at neutral pH forming a negatively charged carboxylate group
A

ACIDIC amino acids

50
Q

accepts protons

A

BASIC amino acids

51
Q

are fully ionized and positvely charged amino acids

A

LYSINE [K]
ARGININE [R]

52
Q

is weakly basic and the free amino acid is uncharged

A

HISTIDINE [H]

53
Q

BASIC amino acids

A

HISTIDINE
ARGININE
LYSINE
ASPARAGINE
TRYTOPHAN

WHeRe Ka Na

54
Q

ESSENTIAL AMINO ACIDS

A

Phenylalanine
Valine
Tryptophan
Threonine
Methionine
Histidine
Arginine
Leucine
Lysine

PVT. TIM HALL

55
Q
  • 21st amino acid
  • Sec and U
  • selenium atom replaces the S in its structural analog, cysteine
  • it is inserted into polypeptides during translation
A

SELENOCYSTEINE

56
Q
  • produced by a specific tRNA and aminoacyl tRNA synthetase, it forms part of an unusual genetic code in these organisms, and is considered the 22nd proteinogenic amino acid
  • Pyl and O
A

PYRROLYSINE

57
Q

RARE AMINO ACIDS

found in collagen

A

4-hydroxyproline
5-hydroxylysine

58
Q

RARE AMINO ACIDS

found in cell walls of bacteria

A

D-Glutamic acid

59
Q

RARE AMINO ACIDS

found in earthworms

A

D-Serine

60
Q

RARE AMINO ACIDS

a neurotransmitter

A

γ-aminobutyric acid

61
Q

RARE AMINO ACIDS

constituent of the vitamin panthothenic acid

A

β-alanine

62
Q

the only optically inactive amino acid

A

GLYCINE

BIOCHEM LEC (33 decks)

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