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T2 - biochem midterm 1 > Unit 2: Chem of Amino Acids, Peptides and proteins > Flashcards

Unit 2: Chem of Amino Acids, Peptides and proteins Flashcards

S:35

1
Q

_______ is a monomeric unit of peptides and proteins

A

amino acids

  • mosty occurs as a L- alpha amino acid
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2
Q

what does pKa mean?

A

when 50% of the functional group has H+ and 50% doesn’t have H

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3
Q

most amino acids occur as ___ amino acids

A

L alpha amino acids

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4
Q

what is the alpha carbon?

A

The carbon that the primary functional group binds to

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5
Q

_____ pKa means that there is a lot of H in the environment and the carbon will hold onto the H

A

Low pKa

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6
Q

____ pKa means that there is not a lot of H in the environment and the fxn group will donate a H

A

High pKa

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7
Q

Phe

A

Phenylalanine

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8
Q

Val

A

Valine

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9
Q

Thr

A

Threonine

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10
Q

Trp

A

tryptophan

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11
Q

Ile

A

Isoleucine

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12
Q

Met

A

Methionine

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13
Q

His

A

Histidine

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14
Q

Arg

A

arginine

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15
Q

Leu

A

Leucine

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16
Q

Lys

A

Lysine

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17
Q

PVT

essential amino acids

A

Phe - phenylalanine
Val - Valine
Threonine - Threonine

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18
Q

TIM

essential amino acids

A

Trp - Tryptophan

Ile - Isoleusine

Met- Methionine

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19
Q

HALL

essential amino acids

A

His- Histidine

Arg - arginine

Leu - Leucine

Lys- Lysine

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20
Q

What two amino acids are not required for protein synthesis ?

are they essential or non essential?

A

Hyl - hydroxylysine

Hyp- hydroxyproline

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21
Q

name the 5 aliphatic amino acids

  • Which are non essential
A

Gly- non

ala - Non

val

leu

Ile

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22
Q

Name the 5 amino acids with hydroxyl fxn groups

- which are essential

A

Thr - Essential

Ser

Tyr

Hyl

Hyp

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23
Q

Name the two amino acids with sulfer fxn group

  • which is essential
A

Cys

Met - Essential

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24
Q

Name the 4 amino acids with a carboxylic/ amide

A

Asp

Glu

Asn

Gln

(all are non-essential

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25
Q

Name the 4 basic amino acids

  • which is non essential
A

Lys

arg

His

Hyl - non essential

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26
Q

Name the 4 aromatic amino acids

A

His

Phe

Trp

Tyr- non-essential

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27
Q

what is a pyrrolidine functional group ?

A

cyclic amine (CH2)4NH

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28
Q

Name the 2 amino acids with an pryrrolidine functional group

A

Pro

Hyp

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29
Q

What is the intermediate / amino acid required for Met

A

homocysteine

  • fxn with B12
    High levels ass. with atherosclerosis
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30
Q

High levels of _____ are ass. with atherosclerosis

A

homocysteine

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31
Q

What vit. does homocysteine fxn with?

A

B12

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32
Q

3 intermediates in biosynthesis of urea

A

ornithine
citrulline
argosuccinic acid

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33
Q

Ornithine is an intermediate for synthesis of _____

A

synthesis of urea

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34
Q

citrulline is an intermediate for synthesis of ____

A

urea

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35
Q

arginosuccinic acid is an intermediate for synthesis of

A

urea

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36
Q

____ is used as a drug for parkinsons disease

A

L-DOPA

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37
Q

L-DOPA is a precursor for biosynthesis of _____

A

catecholamines

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38
Q

Name the three most abundant catecholamines

A

epinephrine
norepinephrine
dopamine

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39
Q

Phenylalanine will produce ____

A

tyrosine

40
Q

Tryosine is a derivative of _____

A

phenylalanine

essential to make a non essential

41
Q

Cathechol decarboxylates to form _____. And is no longer an amino acid then

A

cathecholamine

42
Q

Cathecholamine is a derivative of ____ that underwent decarboxylation

A

cathechol

43
Q

_____ horm increases BMR, protein synthesis and cell proliferation

A

thyroid hormine

44
Q

name the 2 precursors to make thyroid hormone

A

3-monoiodotyrosine

3,5-diiodotyrosine

(need iodine to make thyroid)

45
Q

what non essential amino acid is the base for iodination to make thyroxine

A

tyrosine

46
Q

_____ makes vit B5

A

B-alamine

47
Q

_____ helps with the integrity and fxn of the retina

A

taurine

-beta amino acid

48
Q

______ helps to make bile

A

taurocholic

49
Q

taurocholic’s base is ___

A

taurine

50
Q

Gamma-amnobutyric acid is also known as ____

A

GABA

51
Q

____ inhibites neurotransmitters from glutamate

A

GABA

52
Q

BABA inhibites neurotransmitters from ___

A

glutamate

53
Q

_____ means that the molec. are mirror images of each other

A

enantiomers

54
Q

A chiral molec that deflects polarized light to the left is caled ______

A

levorotatory (l or - )

55
Q

A chiral molec that deflects polarized light to the right is caled ______

A

dextrorotatory ( d or + )

56
Q

_______: molec that possesses both pos. and neg charges

A

Zwitterion

  • amino acids can have both a + / - charge
57
Q

at low pH: there is more ___ charge

A

( + )

- there is more H+ around in the enviro. so molec. wont donate it

58
Q

at high pH: there is more ___ charge

A

(-)

- there is not a lot of H in the enviro., whats to donate it

59
Q

polar molec. are hydro___

A

hydrophilic

60
Q

polar molec are hydrophilic and can make ___ or ____ bonds

A

ionic or hydrogen bonds

61
Q

Non-polar molec. are hydro____

A

hydrophobic

  • they do not have ionic charges
62
Q

If the R-group of an amino acid are aromatic they ahve strong ___

A

UV absorption

63
Q

If an R- group of an amino acid are -OH they can become esterified by _____.

A

phsphorylation

alters the protein fxn

64
Q

If R-group of amino acid are -SH they oxidize to form _______ bonds

A

disulfide

65
Q

Disulfide bonds are usually formed btw two _____ (amino acid)

A

cysteine

non-essential amino acid

66
Q

Disulfide bonds involved in redox rxn of ____

A

antioxidants

67
Q

what does HbAc mean?

A

Hemoglobin adult, one carbohydrate

68
Q

-OH or -NH2 can form glycoproteins by covalently bonding carb _____ bonds

A

glycosidic bonds

: covalent bond that joins carb molec to another group

69
Q

___: the rxn in which a carb is attached to a -OH or other fxn group

A

glycosylation

70
Q

glycohemoglobin means : _____

this is seen in what c.c.?

A

high levels of blood flucose levels

  • diabetes
71
Q

glycohemoglobin is formed by ____ bonds

A

glycosidic bonds

72
Q

peptides are less then _____ amino acids

A

10

73
Q

polypeptides are more then ____ amino acids

A

10

74
Q

Proteins are comprised of many ____

A

polypeptides

75
Q

Glutathione is a tripeptide made up of ___,__& ____ a.a.

A

Glu
cys
gly

76
Q

Glutathione (GSH) is a peptide. Its fxn is ___

A

intracellular antioxidant

77
Q

Peptide substance P is a ______

A

pain neurotransmitter

78
Q

______: is an 11 a.a peptide in the gut, SC and brain

A

Substance P

79
Q

_____: is a vasodilating polypeptide

A

kinins (bradykinin & kallidin)

80
Q

_____ is a vasodilator polypeptide that is derived from proteolytic cleavage

A

kinin

81
Q

_____: is the breakdown of proteins into smaller polypeptides or a.a.
Occurs by the hydrolysis of the peptide bond,

A

Proteolysis

  • breaking off the inactive part
82
Q

Name 3 opiopeptides

A
  1. enkaphalins
  2. B-endorphin
  3. Dynorphin
83
Q

_____: have analgesic actions like opiates

A

opiopeptides

84
Q

____ is an opiopeptide in the SC

A

dynorphin

85
Q

_______ structures dictates specific a.a. sequences

A

primary structures

86
Q

______ structure describes the 3-D structure of protein

A

tertiary structure

87
Q

Fxn of Hb

A

transportation of O2 and CO2

buffers

88
Q

a2B2 is a ___ HbA

A

adult

89
Q

a2y2 is a _____HbA

y=gamma

A

fetal

90
Q

What are three structures on Hb that bind O2

A
  1. Fe
  2. His (F8)
  3. His (E7) –> hinders Co binding
91
Q

R-form of Hb binds to ____

A

O2

92
Q

T-form cannot bind to _____ but can bind to _____

A

cannot bind to O2

Can bind to CO2

93
Q

Ex of _______: binding of first O2 takes the longest. The rest gets progressively faster. bc the binding O2 changes conformation of other subunits

A

cooperative allosterism

94
Q

What is the hemoprotein found in M.

A

myoglobin

95
Q

O2 bound to ____ is a reserve for when pO2 of tissue is low . It then releases for AT synthesis

A

myoglobin

96
Q

______ is the most abundent protein in the body

A

collagen

97
Q

_____ is the most abundant aa in collagen, with lots of ___ &_____

A

glycine

lots of : proline and lysine

T2 - biochem midterm 1 (6 decks)

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