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Biochemistry > Protein and Amino Acid Chemistry > Flashcards

Protein and Amino Acid Chemistry Flashcards

1
Q

storage of protein

A

ferritin, myoglobin

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2
Q

Alcohol-soluble protein in simple protein

A

prolamine

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3
Q

Disulfide bond is also important in maintenance of protein structure

A

Thiol Group containing (Thioether side chain)

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4
Q

Example of aromatic

A
  • Phenylalanine
  • Tryptophan
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5
Q

Solubility of Amino Acid

A

All amino acid are soluble in water

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6
Q

example of proteins for cell signaling

A

membrane receptors like insulin receptors

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7
Q

made up of AMINO ACIDS ONLY

A

simple protein

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8
Q

1 gram of protein is equal to

A

4 cals of energy

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9
Q

the simplest and smallest amino acid

A

Glycine

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10
Q

example of lipoprotein

A

LDL, HDL

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11
Q

from asparagus, 1st amino acid discovered

A

Asparagine

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12
Q
  • elongated
  • Tough
  • Insoluble in water
  • Arranged around a single axis to form a fiber
  • Involved in structural functions
  • E.g. Collagen, Keratin
A

fibrous proteins

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13
Q

Interactions between acidic and basic amino acids results in the formation of ionic bond

A

negatively charged polar R groups

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14
Q

are complex organic nitrogenous substances with very high molecular weights, found in all plant and animal cells, consisting largely or entirely of alpha-amino acids united in peptide linkages.

A

proteins

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15
Q

Hydroxyl-containing (OH) Amino Acids

A

o Serine
o Threonine
o Tyrosine

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16
Q

glutelin found in rice

A

oryzenin

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17
Q

Ring of Proline

A

pyrolidine ring

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18
Q

Also called Basic amino acids

A

Positively Charged Polar R Groups

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19
Q

When two cysteine residues combine, a strong disulfide bond is
formed and cystine is the resulting product

A

Thiol Group containing (Thioether side chain)

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20
Q

Arginine contains _____ group

A

guanido

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21
Q

Alpha carbon is ________ except for glycine

A

ASYMMETRIC

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22
Q

Precursor of niacin, serotonin, melatonin, indole, skatole in amino acid

A

tryptophan

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23
Q
  • Insoluble in water
  • Soluble in aqueous salt solution
  • Heat coagulable
A

globulin

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24
Q

protective in protein

A

blood clotting factors, Immunoglobulins, interferon

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25
Q

made up of AMINO ACIDS + OTHER SUBSTANCES (PROSTHETIC GROUP)

A

conjugated proteins

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26
Q

major source of biological membranes

A

transmembrane proteins (integral proteins) or peripheral proteins

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27
Q

Impairment in human
selenoproteins have been implicated in

A
  • tumorigenesis
  • atherosclerosis
  • associated with selenium deficiency
    cardiomyopathy
    (Keshan Disease)
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28
Q

If amino acids possess both positive and negative charge, they are termed as

A

amphoteric molecules

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29
Q

Amino Acids with –SH in the R-group:

A

CYSTEINE

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30
Q

Referred to as NEUTRAL amino acids containing hydrocarbon R groups

A

Amino Acids with NONPOLAR or HYDROPHOBIC R Groups

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31
Q

Ultraviolet Absorption Spectrum of Amino Acid

A

determined solely by Phe, Tyr and Trp

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32
Q

What are the Positively Charged Polar R Groups

A

Love All Humans
Lysine
Arginine
Histidine

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33
Q

It is a seed protein

A

prolamine

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34
Q

example of phosphoprotein

A

casein

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35
Q

transport in protein

A

hgb, lipoproteins, transferrin

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36
Q

pK values of the α amino groups (NH2) = all near

A

9.4

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37
Q

Side chain of Alanine

A

Methyl group

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38
Q

it makes the major contribution to the ability of most proteins to absorb light in the region of 280 nm

A

Tryptophan

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39
Q

contractile/motile in protein

A

actin, myosin

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40
Q

responsible for the buffering capacity of hemoglobin

A

imidazole group

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41
Q

Important in maintaining protein structure

A

negatively charged polar R groups

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42
Q

Sites of Phosphorylation reactions

A

Hydroxyl-containing Amino Acids

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43
Q

proteins for mechanical support

A

Collagen and Keratin

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44
Q

Amino Acids with Hydroxyl Group (OH)

A

Ser, Tara, Tagay (alcohol)

Serine
Threonine
Tyrosine

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45
Q

tryptophan has what kind of ring

A

indole ring (has a dual ring)

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46
Q

what are the negatively charged polar R groups

A

Angry Girls

Aspartic acid
Glutamic acid

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47
Q

central carbon in amino acid

A

alpha carbon

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48
Q
  • Simplest protein
  • Basic
  • Soluble in water
  • Dilute ammonia, acid and alkali
  • Found in spermatozoa
A

protamine

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49
Q

It is a plant protein

A

glutelin

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50
Q

enzymes of protein

A

dehydrogenases, kinases

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51
Q

Fully dissociated forms of amino acids are _____ NEGATIVE

A

ALWAYS

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52
Q

example of chromoprotein

A

hemoglobin

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53
Q

Amide (CONH2) derivatives of Glutamate and Aspartate

A

o Glutamine
o Asparagine

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54
Q

Building blocks of proteins

A

amino acid

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55
Q

Least soluble simple protein

A

Albuminoid or Scleroprotein

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56
Q

proteins responsible for the relaxation and contraction of muscles

A

actin and myosin

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57
Q

Thiol (-SH) Group containing

A

Cysteine

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58
Q

pH 11 and above in acid-base of amino acid means

A

ALAKALINIC MEDIUM

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59
Q

Amino Acids with –OH in the R-group:

A

SERINE
TYROSINE
THREONINE

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60
Q

Have a zero net charge at neutral pH

A

Uncharged Polar

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61
Q
  • circular
  • Involved in mobile and dynamic functions
  • For transport purposes
  • E.g. Enzymes, hemoglobin, plasma proteins
A

globular proteins

62
Q

what are the 7 simple proteins?

A
  1. Albumin
  2. Globulin
  3. Glutelin
  4. Prolamine
  5. Albuminoid/Scleroprotein
  6. Protamine
  7. Histone
63
Q

Basic Amino Acids:

A

LYSINE
ARGININE
HISTIDINE

64
Q

types of hydrocarbon side chains wherein there is a ring

A

aromatic

65
Q

prosthetic group of phosphoprotein

A

phosphoric acid residue

66
Q

referred to as the “helix breaker.”

A

proline

67
Q

Contains the sulfhydryl (-SH) group

A

Thiol Group containing (Thioether side chain)

68
Q

chemical messenger in amino acid

A

GABA, serotonin

69
Q
  • Soluble in dilute acid and alkalis
  • Heat coagulable
A

glutelin

70
Q

21st L-α-amino acid

A

Selenocysteine

71
Q

what amino acids are present in proteins

A

Only L- α amino acids are present in proteins

72
Q

phenylalanine has what kind of ring

A

benzene ring

73
Q

Protein Hormones

A

Insulin
Thyrotropin
Somatotropin (Growth Hormone)
Luteinizing Hormone
Follicle Stimulating Hormone

74
Q
  • Basic protein
  • Soluble in water
  • Dilute acid and alkali
  • Found in combination with DNA
A

histone

75
Q

the source of S-adenosylmethionine (SAM) which is the methyl group donor in methylation reactions

A

methionine

76
Q

2 types of hydrocarbon side chains

A
  1. aromatic
  2. aliphatic
77
Q

Side chain of Glycine

A

hydrogen

78
Q

Contain polar hydroxyl groups

A

Hydroxyl-containing Amino Acids

79
Q

NONPOLAR or HYDROPHOBIC R Groups

A

All Girls Pay Large Value In Pretty Thick Make up

Alanine (unbranched)
Glycine (unbranched)
Proline (branched)
Leucine (branched)
Valine (branched)
Isoleucine (branched)
Phenylalanine (aromatic)
Tryptophan (aromatic)
Methionine (branched)

80
Q

storage form of iron

A

ferritin

81
Q

Important factor in protein structure

A

Uncharged Polar

82
Q

All amino acids will have a chiral carbon with the exception of

A

GLYCINE

83
Q

sweet taste

A

Glycine

84
Q

types of hydrocarbon side chains wherein there is a straight or linear chain

A

aliphatic

85
Q

in amino acid, what are the four different groups attached in the central carbon

A
  1. a basic amino group (-NH2)
  2. an acidic carboxyl group (-COOH)
  3. a hydrogen atom (-H)
  4. a distinctive side chain (-R)
86
Q

examples of aliphatic branched

A

o Valine
o Leucine
o Isoleucine
o Methionine
o Proline

87
Q

Acid-Base Properties of Amino Acid

A

Amino Group = can become positively charged when it accepts a proton

Carboxyl Group = can become negatively charged when it donates a proton

88
Q

what are the UNCHARGED POLAR R Groups

A

Some Times Clingy Girls Are Tenacious

Serine
Threonine
Cysteine
Glutamine
Asparagine
Tyrosine

89
Q

it is the primary source of urinary ammonia

A

Glutamine

90
Q

Precursor of histamine in amino acid

A

histidine

91
Q

Ring of Histidine

A

imidazole ring

92
Q
  • Soluble in water
  • Dilute aqueous salt solution
  • Heat coagulable
A

albumin

93
Q

prosthetic group of chromoprotein

A

prosthetic group that gives color

94
Q

neurotransmitters that are derived from different amino acids:

A
  • Epinephrine
  • Norepinephrine
95
Q

Taste of Amino Acid

A

either be sweet, bitter or tasteless

96
Q

hair, scales, horns, wool, nails and feathers

A

keratin

97
Q

Classification based on Composition, Physical and Chemical Properties of the Protein

A

simple proteins
conjugated proteins
derived proteins

98
Q

Have functional groups capable of hydrogen bonding with water

A

Uncharged Polar

99
Q

Genetic code specifies _____ alpha amino acids

A

20 L

100
Q

prosthetic group of nucleoprotein

A

nucleic acid

101
Q

state the 20 amino acid

A

Gly Ala Pro Value
Iso Met Ser 3 sis
As Glu LiAr Hi
As Glu Penny Tire Trip

Glycine, Alanine, Proline, Valine, Leucine, Isoleucine, Methionine, Serine, Threonine, Cysteine, Asparagine, Glutamine, Lysine, Arginine, Histidine, Aspartate, Glutamate, Phenylalanine, Tyrosine, Tryptophan

102
Q

prosthetic group of lipoprotein

A

lipids

103
Q

Ring of Tyrosine

A

phenol ring

104
Q

transports oxygen

A

hemoglobin

105
Q

metabolic intermediates of amino acid

A

Arg, citrulline, ornithine – urea cycle

106
Q

structural in protein

A

collagen, proteoglycans, elastin

107
Q

first isolated from cheese

A

Tyrosine

108
Q

A protein can only be called protein if that _____ chain is made up of ____ amino acids. Less than
50, it is only a ______

A

polypeptide; 50 or more; polypeptide

109
Q

Precursor of carnitine in amino acid

A

Lysine and Methionine

110
Q

TYPES OF INTERACTIONS ENTERED INTO BY THE DIFFERENT R GROUPS (SIDE CHAINS) OF AMINO ACIDS

A
  1. Hydrogen Bonding
  2. Ionic Interaction
  3. Hydrophobic interaction of Nonpolar R Groups
  4. Disulfide Bonds
111
Q

The 2 amino acids have R groups with a net negative charge at pH 7.0, each of which has a second carboxyl group

A

negatively charged polar R groups

112
Q

pK values of the α carboxylic acid groups (COOH) = usually lie in a small range around ___

A

2.2

113
Q

regulatory in protein

A

DNA-binding proteins

114
Q

Important in detoxification of ammonia

A

Amide (CONH2) derivatives of Glutamate and Aspartate

115
Q

Ring of Tryptophan

A

Indole ring

116
Q

example of Albuminoid or Scleroprotein

A

collagen and keratin

117
Q

they are mainly proteins in nature, thereby proteins could serve as catalysts

A

enzymes

118
Q

Amino Acids with COOH in the R-group:

A

ASPARTIC ACID
GLUTAMIC ACID

119
Q

Ring of Phenylalanine

A

phenyl ring

120
Q

Precursor of thyroxine, epinephrine, melanin in amino acid

A

Phe and Tyr

121
Q

seed protein that can be found in corns

A

zein

122
Q

Classification Based on Shape and Certain Physical Characteristics of the Protein

A

fibrous proteins
globular proteins

123
Q

first isolated from wheat gluten

A

Glutamate

124
Q

Important in formation of mucin

A

Hydroxyl-containing Amino Acids

125
Q

prosthetic group of metalloprotein

A

metals or minerals

126
Q

2 types of aliphatic

A
  • aliphatic unbranched
  • aliphatic branched
127
Q

derived proteins

A

a. Primary Derived
b. Secondary Derived

128
Q

in wheat, what do you call the glutelin that can be found? and the seed protein?

A

glutelin = glutenin
seed protein = gliadin

129
Q

Appearance of Amino Acid

A

do not absorb visible light and thus are
colorless.

130
Q

Classification Based on Biologic Functions

A
  1. Enzymes
  2. Storage
  3. Regulatory
  4. Structural
  5. Protective
  6. Transport
  7. Contractile or Motile
131
Q

most abundant, 25% protein of the body

A

collagen

132
Q

The side chain of GLYCINE in amino acid is

A

hydrogen

133
Q

It is an animal protein

A

Albuminoid or Scleroprotein

134
Q

If there are four different atoms attached to a carbon, that carbon is named as

A

chiral carbon

135
Q

prosthetic group of glycoprotein and mucoprotein

A

carbohydrates

136
Q

important control elements that silence a
specific DNA of a cell

A

suppressor or repressor proteins

137
Q

examples of aliphatic unbranched

A
  • Glycine
  • Alanine
138
Q

3 Types of POLAR AMINO ACIDS:

A
  1. Uncharged Polar- neutral or no charge
  2. Positively Charged Polar- basic
  3. Negatively Charged Polar- acidic
139
Q

Precursor of heme, purine, creatine, glutathione, hippuric acid in amino acid

A

glycine

140
Q

Site of Glycosylation reactions

A

Hydroxyl-containing Amino Acids

141
Q

it contains the imidazole group

A

Histidine

142
Q

Nonpolar Amino Acids:

A

All Girls Pay Large Value In Pretty Thick Make ups

ALANINE
GLYCINE PHENYLALANINE
LEUCINE
VALINE
ISOLEUCINE
PROLINE
TRYPTOPHAN
METHIONINE

143
Q

This is essential for the orderly growth and differentiation of cells.

A

suppressor or repressor proteins

144
Q

what amino acids absorb high-wavelength (250-290 nm) ultraviolet light

A

tyrosine, phenylalanine, and tryptophan

145
Q

Between an acidic (-COOH) amino acid and a basic (NH3+) amino acid

A

Ionic Interaction

146
Q

Acidic Amino Acids:

A

ASPARTIC ACID
GLUTAMIC ACID

147
Q

example of metalloprotein

A

cytochrome

148
Q

Melting Point of Amino Acid

A

Amino acids have a high melting point → Usually
200 degree Celsius and above

149
Q

a property that promotes hydrophobic interactions

A

“oily”, or lipid-like

150
Q

ionic bond is also called

A

also called salt bond, electrostatic bond

151
Q

Aromatic Amino Acids

A

Phenylalanine
Tyrosine
Tryptophan
Histidine
Proline

152
Q

antibodies are derived from _____, which are
proteins.

A

gamma globulins

Biochemistry (5 decks)

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