Protein and Amino Acid Chemistry Flashcards
(152 cards)
1
Q
storage of protein
A
ferritin, myoglobin
2
Q
Alcohol-soluble protein in simple protein
A
prolamine
3
Q
Disulfide bond is also important in maintenance of protein structure
A
Thiol Group containing (Thioether side chain)
4
Q
Example of aromatic
A
- Phenylalanine
- Tryptophan
5
Q
Solubility of Amino Acid
A
All amino acid are soluble in water
6
Q
example of proteins for cell signaling
A
membrane receptors like insulin receptors
7
Q
made up of AMINO ACIDS ONLY
A
simple protein
8
Q
1 gram of protein is equal to
A
4 cals of energy
9
Q
the simplest and smallest amino acid
A
Glycine
10
Q
example of lipoprotein
A
LDL, HDL
11
Q
from asparagus, 1st amino acid discovered
A
Asparagine
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
13
Q
Interactions between acidic and basic amino acids results in the formation of ionic bond
A
negatively charged polar R groups
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
15
Q
Hydroxyl-containing (OH) Amino Acids
A
o Serine
o Threonine
o Tyrosine
16
Q
glutelin found in rice
A
oryzenin
17
Q
Ring of Proline
A
pyrolidine ring
18
Q
Also called Basic amino acids
A
Positively Charged Polar R Groups
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)
20
Q
Arginine contains _____ group
A
guanido
21
Q
Alpha carbon is ________ except for glycine
A
ASYMMETRIC
22
Q
Precursor of niacin, serotonin, melatonin, indole, skatole in amino acid
A
tryptophan
23
Q
- Insoluble in water
- Soluble in aqueous salt solution
- Heat coagulable
A
globulin
24
Q
protective in protein
A
blood clotting factors, Immunoglobulins, interferon
25
made up of AMINO ACIDS + OTHER SUBSTANCES (PROSTHETIC GROUP)
conjugated proteins
26
major source of biological membranes
transmembrane proteins (integral proteins) or peripheral proteins
27
Impairment in human
selenoproteins have been implicated in
- tumorigenesis
- atherosclerosis
- associated with selenium deficiency
cardiomyopathy
(Keshan Disease)
28
If amino acids possess both positive and negative charge, they are termed as
amphoteric molecules
29
Amino Acids with –SH in the R-group:
CYSTEINE
30
Referred to as NEUTRAL amino acids containing hydrocarbon R groups
Amino Acids with NONPOLAR or HYDROPHOBIC R Groups
31
Ultraviolet Absorption Spectrum of Amino Acid
determined solely by Phe, Tyr and Trp
32
What are the Positively Charged Polar R Groups
Love All Humans
Lysine
Arginine
Histidine
33
It is a seed protein
prolamine
34
example of phosphoprotein
casein
35
transport in protein
hgb, lipoproteins, transferrin
36
pK values of the α amino groups (NH2) = all near
9.4
37
Side chain of Alanine
Methyl group
38
it makes the major contribution to the ability of most proteins to absorb light in the region of 280 nm
Tryptophan
39
contractile/motile in protein
actin, myosin
40
responsible for the buffering capacity of hemoglobin
imidazole group
41
Important in maintaining protein structure
negatively charged polar R groups
42
Sites of Phosphorylation reactions
Hydroxyl-containing Amino Acids
43
proteins for mechanical support
Collagen and Keratin
44
Amino Acids with Hydroxyl Group (OH)
Ser, Tara, Tagay (alcohol)
Serine
Threonine
Tyrosine
45
tryptophan has what kind of ring
indole ring (has a dual ring)
46
what are the negatively charged polar R groups
Angry Girls
Aspartic acid
Glutamic acid
47
central carbon in amino acid
alpha carbon
48
- Simplest protein
- Basic
- Soluble in water
- Dilute ammonia, acid and alkali
- Found in spermatozoa
protamine
49
It is a plant protein
glutelin
50
enzymes of protein
dehydrogenases, kinases
51
Fully dissociated forms of amino acids are _____ NEGATIVE
ALWAYS
52
example of chromoprotein
hemoglobin
53
Amide (CONH2) derivatives of Glutamate and Aspartate
o Glutamine
o Asparagine
54
Building blocks of proteins
amino acid
55
Least soluble simple protein
Albuminoid or Scleroprotein
56
proteins responsible for the relaxation and contraction of muscles
actin and myosin
57
Thiol (-SH) Group containing
Cysteine
58
pH 11 and above in acid-base of amino acid means
ALAKALINIC MEDIUM
59
Amino Acids with –OH in the R-group:
SERINE
TYROSINE
THREONINE
60
Have a zero net charge at neutral pH
Uncharged Polar
61
- circular
- Involved in mobile and dynamic functions
- For transport purposes
- E.g. Enzymes, hemoglobin, plasma proteins
globular proteins
62
what are the 7 simple proteins?
1. Albumin
2. Globulin
3. Glutelin
4. Prolamine
5. Albuminoid/Scleroprotein
6. Protamine
7. Histone
63
Basic Amino Acids:
LYSINE
ARGININE
HISTIDINE
64
types of hydrocarbon side chains wherein there is a ring
aromatic
65
prosthetic group of phosphoprotein
phosphoric acid residue
66
referred to as the “helix breaker.”
proline
67
Contains the sulfhydryl (-SH) group
Thiol Group containing (Thioether side chain)
68
chemical messenger in amino acid
GABA, serotonin
69
- Soluble in dilute acid and alkalis
- Heat coagulable
glutelin
70
21st L-α-amino acid
Selenocysteine
71
what amino acids are present in proteins
Only L- α amino acids are present in proteins
72
phenylalanine has what kind of ring
benzene ring
73
Protein Hormones
Insulin
Thyrotropin
Somatotropin (Growth Hormone)
Luteinizing Hormone
Follicle Stimulating Hormone
74
- Basic protein
- Soluble in water
- Dilute acid and alkali
- Found in combination with DNA
histone
75
the source of S-adenosylmethionine (SAM) which is the methyl group donor in methylation reactions
methionine
76
2 types of hydrocarbon side chains
1. aromatic
2. aliphatic
77
Side chain of Glycine
hydrogen
78
Contain polar hydroxyl groups
Hydroxyl-containing Amino Acids
79
NONPOLAR or HYDROPHOBIC R Groups
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
storage form of iron
ferritin
81
Important factor in protein structure
Uncharged Polar
82
All amino acids will have a chiral carbon with the exception of
GLYCINE
83
sweet taste
Glycine
84
types of hydrocarbon side chains wherein there is a straight or linear chain
aliphatic
85
in amino acid, what are the four different groups attached in the central carbon
1. a basic amino group (-NH2)
2. an acidic carboxyl group (-COOH)
3. a hydrogen atom (-H)
4. a distinctive side chain (-R)
86
examples of aliphatic branched
o Valine
o Leucine
o Isoleucine
o Methionine
o Proline
87
Acid-Base Properties of Amino Acid
Amino Group = can become positively charged when it accepts a proton
Carboxyl Group = can become negatively charged when it donates a proton
88
what are the UNCHARGED POLAR R Groups
Some Times Clingy Girls Are Tenacious
Serine
Threonine
Cysteine
Glutamine
Asparagine
Tyrosine
89
it is the primary source of urinary ammonia
Glutamine
90
Precursor of histamine in amino acid
histidine
91
Ring of Histidine
imidazole ring
92
- Soluble in water
- Dilute aqueous salt solution
- Heat coagulable
albumin
93
prosthetic group of chromoprotein
prosthetic group that gives color
94
neurotransmitters that are derived from different amino acids:
* Epinephrine
* Norepinephrine
95
Taste of Amino Acid
either be sweet, bitter or tasteless
96
hair, scales, horns, wool, nails and feathers
keratin
97
Classification based on Composition, Physical and Chemical Properties of the Protein
simple proteins
conjugated proteins
derived proteins
98
Have functional groups capable of hydrogen bonding with water
Uncharged Polar
99
Genetic code specifies _____ alpha amino acids
20 L
100
prosthetic group of nucleoprotein
nucleic acid
101
state the 20 amino acid
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
prosthetic group of lipoprotein
lipids
103
Ring of Tyrosine
phenol ring
104
transports oxygen
hemoglobin
105
metabolic intermediates of amino acid
Arg, citrulline, ornithine – urea cycle
106
structural in protein
collagen, proteoglycans, elastin
107
first isolated from cheese
Tyrosine
108
A protein can only be called protein if that _____ chain is made up of ____ amino acids. Less than
50, it is only a ______
polypeptide; 50 or more; polypeptide
109
Precursor of carnitine in amino acid
Lysine and Methionine
110
TYPES OF INTERACTIONS ENTERED INTO BY THE DIFFERENT R GROUPS (SIDE CHAINS) OF AMINO ACIDS
1. Hydrogen Bonding
2. Ionic Interaction
3. Hydrophobic interaction of Nonpolar R Groups
4. Disulfide Bonds
111
The 2 amino acids have R groups with a net negative charge at pH 7.0, each of which has a second carboxyl group
negatively charged polar R groups
112
pK values of the α carboxylic acid groups (COOH) = usually lie in a small range around ___
2.2
113
regulatory in protein
DNA-binding proteins
114
Important in detoxification of ammonia
Amide (CONH2) derivatives of Glutamate and Aspartate
115
Ring of Tryptophan
Indole ring
116
example of Albuminoid or Scleroprotein
collagen and keratin
117
they are mainly proteins in nature, thereby proteins could serve as catalysts
enzymes
118
Amino Acids with COOH in the R-group:
ASPARTIC ACID
GLUTAMIC ACID
119
Ring of Phenylalanine
phenyl ring
120
Precursor of thyroxine, epinephrine, melanin in amino acid
Phe and Tyr
121
seed protein that can be found in corns
zein
122
Classification Based on Shape and Certain Physical Characteristics of the Protein
fibrous proteins
globular proteins
123
first isolated from wheat gluten
Glutamate
124
Important in formation of mucin
Hydroxyl-containing Amino Acids
125
prosthetic group of metalloprotein
metals or minerals
126
2 types of aliphatic
- aliphatic unbranched
- aliphatic branched
127
derived proteins
a. Primary Derived
b. Secondary Derived
128
in wheat, what do you call the glutelin that can be found? and the seed protein?
glutelin = glutenin
seed protein = gliadin
129
Appearance of Amino Acid
do not absorb visible light and thus are
colorless.
130
Classification Based on Biologic Functions
1. Enzymes
2. Storage
3. Regulatory
4. Structural
5. Protective
6. Transport
7. Contractile or Motile
131
most abundant, 25% protein of the body
collagen
132
The side chain of GLYCINE in amino acid is
hydrogen
133
It is an animal protein
Albuminoid or Scleroprotein
134
If there are four different atoms attached to a carbon, that carbon is named as
chiral carbon
135
prosthetic group of glycoprotein and mucoprotein
carbohydrates
136
important control elements that silence a
specific DNA of a cell
suppressor or repressor proteins
137
examples of aliphatic unbranched
- Glycine
- Alanine
138
3 Types of POLAR AMINO ACIDS:
1. Uncharged Polar- neutral or no charge
2. Positively Charged Polar- basic
3. Negatively Charged Polar- acidic
139
Precursor of heme, purine, creatine, glutathione, hippuric acid in amino acid
glycine
140
Site of Glycosylation reactions
Hydroxyl-containing Amino Acids
141
it contains the imidazole group
Histidine
142
Nonpolar Amino Acids:
All Girls Pay Large Value In Pretty Thick Make ups
ALANINE
GLYCINE PHENYLALANINE
LEUCINE
VALINE
ISOLEUCINE
PROLINE
TRYPTOPHAN
METHIONINE
143
This is essential for the orderly growth and differentiation of cells.
suppressor or repressor proteins
144
what amino acids absorb high-wavelength (250-290 nm) ultraviolet light
tyrosine, phenylalanine, and tryptophan
145
Between an acidic (-COOH) amino acid and a basic (NH3+) amino acid
Ionic Interaction
146
Acidic Amino Acids:
ASPARTIC ACID
GLUTAMIC ACID
147
example of metalloprotein
cytochrome
148
Melting Point of Amino Acid
Amino acids have a high melting point → Usually
200 degree Celsius and above
149
a property that promotes hydrophobic interactions
“oily”, or lipid-like
150
ionic bond is also called
also called salt bond, electrostatic bond
151
Aromatic Amino Acids
Phenylalanine
Tyrosine
Tryptophan
Histidine
Proline
152
antibodies are derived from _____, which are
proteins.
gamma globulins
