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biochem > (M) Amino Acids Vid Lec based > Flashcards

(M) Amino Acids Vid Lec based Flashcards

1
Q

The building block of peptides and proteins

A

amino acids

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2
Q

Where does the body get energy from when there is an insufficient amount of calories in fats?

A

protein

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3
Q

how many cal of energy in protein

A

4 cal / g

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4
Q

how many cal of energy in lipids

A

9 cal / g

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5
Q

a compound that participates in a chemical reaction which produces a compound

A

precursor

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6
Q

this is the starting material for heme synthesis

A

glycine

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7
Q

this gives the blood the ability to carry oxygen

A

heme

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8
Q

precursor for glutathione

A

glycine

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9
Q

function of glutathione

A

anti-oxidant

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10
Q

precursor for serotonin

A

tryptophan

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11
Q

precursor for histamine (allergies)

A

histidine

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12
Q

function of amino acids that plays a role in the activation / inactivation of enzymes

A

components of other biologically active constituents

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13
Q

enumerate the 4 different groups attached to the central carbon atom

A

amino group (NH2)
Carboxyl group (-COOH)
Hydrogen (-H)
Distinctive side chain (-R)

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14
Q

This is where the 4 different groups attach

A

second carbon / alpha carbon

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14
Q

what do you call a carbon atom that has 4 different subtituents

A

chiral / asymmetric carbon

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14
Q

the only amino acid that is not chiral

A

glycine

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15
Q

why is glycine not chiral

A

it has two H atoms

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16
Q

the two distinguishable isomers

A

L and D Phenylalanine

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17
Q

isomer that are found in bacterial cell walls and some antibiotics

A

D-stereoisomers

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18
Q

isomer that is oriented to the right side

A

D-Phenylalanine

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19
Q

isomer oriented to the left side

A

L-Phenylalanine

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20
Q

T or F
The R group determines the structure and function of amino acid molecules

A

F
protein molecules

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21
Q

T or F
R group varies in each amino acid, they can be either alcohol or hydrocarbon side chains

A

T

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22
Q

This defines the shape of the protein and how they interact with the environment

A

R groups

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23
Q

side chains that repel water

A

nonpolar side chains

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24
Q

side chains that love water

A

polar side chains

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25
Q

Are polar side chains in the interior or surfaces of the protein?

A

surface

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26
Q

Are nonpolar side chains in the interior or surfaces of the protein?

A

interior

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27
Q

These are neutral amino acids

A

nonpolar and polar uncharged (both have no charges)

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28
Q

what causes nonpolar amino acids to be hydrophobic

A

the hydrocarbon molecules (C & H)

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29
Q

what are aliphatic R groups made out of

A

alkyl groups (CH3)

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30
Q

This aliphatic r group has no chiral carbon

A

Gly

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31
Q

the only true aliphatic R groups

A

Ala, Val, Leu, Ile

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32
Q

smallest and simplest amino acid

A

Gly

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33
Q

isomer of leucine

A

isoleucine

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34
Q

T or F
the increasing amount of branching in aliphatic R groups are inversely proportional to how hydrophobic it is

A

F directly proportional (why though, like what does branching have to do with it ??)

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35
Q

First amino acid in the sequence

Edit: I think it is also the First amino acid in translation process

A

methionine

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36
Q

cyclic aliphatic R group

A

proline

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37
Q

what do you call the five membered rings in proline

A

pyrolibine

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38
Q

what is the rigidity of the pyrolibine for

A

protein structure (collagen)

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39
Q

What causes Methionine to by hydrophobic

A

Sulfur

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40
Q

Type of nonpolar amino acids that is made up of carbon and hydrogen, and has rings

A

aromatic R groups

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41
Q

nonpolar aromatic r group which is linked to beta carbon

A

phenyl group (phenol at indole din)

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42
Q

what is the phenyl group a substituent of

A

methylene

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43
Q

nonpolar aromatic r group that has an electronegative atom in the ring system

A

Tryptophan

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44
Q

What do you call the ring in tryptophan

A

indole ring

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45
Q

least hydrophobic of the 3 aromatic amino acid side chain

A

Tyrosine

46
Q

phenylalanine with aromatic OH group (phenolic OH)

A

Tyrosine

47
Q

most hydrophobic out of the aromatic amino acid side chains

A

phenylalanine

48
Q

Where does aromatic amino acids absorb light

A

near the UV region of EM spectrum (250-300 nm)

49
Q

what are the absorbed UV light used for

A

detection and quantification of proteins

50
Q

Has the highest molar absorptivity

A

Trp

51
Q

enumerate the lowest to highest molar absorptivity

A

Phe, Tyr, Trp

52
Q

also absorbs within the UV range but much less than aromatics

A

disulfide bonds

53
Q

polar groups that have zero net charge or neutral pH

A

uncharged R groups

54
Q

These are aliphatic OH groups not ionizable in pH range 1-13

A

Ser and Thr

55
Q

first amino acid discovered

A

Asparagine

56
Q

Very polar uncharged R groups that cannot be ionized

A

Ser, Thr, Asn, Gln

57
Q

uncharged r group that is not very polar and can be ionized

A

Cys

58
Q

the difference between cysteine and serine

A

cysteine has a thiol group

59
Q

relevant pH range of thiol to lose its proton

A

pKa of about 8.5 (indi ko din masyado gets ito pero sabi ni madam eh)

60
Q

what is formed by combining two cysteines

A

cystine

61
Q

amino acids that are strongly polar, found at the exterior surface of the protein

A

positively charged R groups/polar basic

62
Q

What atom does positively charged R groups contain that accepts protons, making it bear a fully positive charge

A

nitrogen atom

63
Q

most basic positively charged R group

A

Arg / guanidino group

64
Q

positively charged r group that is from am ε-amino group (primary amino group)

A

Lys

65
Q

imidazole functional group (has 2 N atoms in 5-membered unsaturated ring)

A

His

66
Q

least basic, almost neutral positively charged r group

A

His

67
Q

Polar amino acids that contains a carboxylic acid (COO-) as part of their side chain

A

negative charged r groups

68
Q

Found in several proteins including mammalian glutathione peroxidase

A

selenocysteine

69
Q

what inserts selenocysteine into proteins

A

UGA

70
Q

The difference between cysteine and selenocysteine

A

sulfur atom is replaced by selene atom

71
Q

found in monomethylamine methyltransferase

A

pyrrolysine

72
Q

Where is pyrrolysine from

A

methanosaricina bakeri (fresh water microbe)

73
Q

What incorporates pyrrolisine in the protein

A

UAG

74
Q

where is pyrrolisine found

A

a few archaea and eubacteria, usually in microbes

75
Q

Type of interaction wherein -OH group is binded to a carboxylic group

A

hydrogen bonding

76
Q

Type of interaction wherein -COOH is bonded to an amino group

A

ionic interaction

77
Q

Type of interaction between two nonpolar r groups

A

hydrophobic interaction of nonpolar r groups

78
Q

Type of interaction between two sulfurs

A

disulfide bonds

79
Q

Form of amino acid wherein both the carboxyl and amino group are neither negative nor positive

A

unionized form

80
Q

form of amino acid that doesn’t exist in the body, for computation purposes only

A

unionized form

81
Q

form of amino acid that exists in the body

A

dipolar or zwitterion form

82
Q

what is the charge of the amino group and carboxyl group in dipolar / zwitterion form

A

Amino group → POSITIVELY CHARGED
Carboxyl group → NEGATIVELY CHARGED

83
Q

This is when equal amounts of positive and negative charge are present at the same time

A

electrically neutral

84
Q

T or F
charges are directly proportional to solubility

A

T

85
Q

This means that all hydrogen are attached

A

fully protonated

86
Q

Charge of amino group in fully protonated pH 1

A

positive

87
Q

This means that all hydrogen are removed

A

Fully ionized / Dissociated or Deprotonated pH 11

88
Q

charge of carboxyl and amino group in fully ionized form

A

Carboxyl group → NEGATIVELY CHARGED
Amino group → Not positively charged

89
Q

the gradual addition or removal of protein

A

Acid and base titration of amino acids

90
Q

T or F
titration cannot predict the charge of an amino acid in a given solution with a unknown pH

A

T (kasi need na known yun pH)

91
Q

T or F

At low pH of 1.0 the carboxylic and group is protonated.

A

T

92
Q

T or F

in titration, as the pH increases, the carboxylic acid group gains its hydrogen to form zwitterion form (usually permits 7 to 9 pH)

A

F (loses)

93
Q

T or F
At basic pH, titration causes the amino group to lose its hydrogen

A

T

94
Q

this is the pH at which the NET charge on a molecule is ZERO

A

isoelectric point (PI)

95
Q

If pH < pI, what is the net charge

A

positive

96
Q

If pH > pI, what is the net charge

A

negative

97
Q

it is computed as the pH exactly halfway between the two pKa values surrounding the zero net charge

A

PI value

98
Q

the equivalence point on the titration curve

A

average of pI

99
Q

we need the ____to compute for the isoelectric point whether the amino acid can take up or donate to a proton

A

pKa

100
Q

is the amino acid protonated or deprotonated when pH solution is less than the pKa?

A

protonated (+)

101
Q

is the amino acid protonated or deprotonated when pH solution is greater than the pKa?

A

deprotonated (-)

102
Q

How many pKa’s for neutral side chains?

A

2

103
Q

two pKa’s for neutral side chains

A

1 carboxyl
1 amino group

104
Q

T or F

All amino acids have at least 3 ionizable groups

A

F 2

105
Q

T or F

pKa1 is the pka of NH3 group

A

F (COOH)

106
Q

T or F

pKa3 is the pKa of side chain varies (R group)

A

T

107
Q

T or F
pKa2 is the pKa of NH3 group

A

T

108
Q

pKa’s used for amino acids with acidic side chains

A

pKa1 and pKa2

109
Q

pKa’s used for amino acids with basic side chains

A

pKa2 and pKa3

110
Q

form that is the most positively charged happens at low ph; pH 1

A

cationic form

111
Q

form that exists at high pH (12)

A

ionic form

112
Q

You have reached the end of this week’s flash cards

A

Hug nath the following day or you and ur family will be cursed for the next 3 generations

113
Q

Type of ring that phenylalanine have

A

Phenyl ring

114
Q

Type of ring that tyrosine have

A

Phenol ring

biochem (31 decks)

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