(M) Amino Acids Vid Lec based Flashcards
1
Q
The building block of peptides and proteins
A
amino acids
2
Q
Where does the body get energy from when there is an insufficient amount of calories in fats?
A
protein
3
Q
how many cal of energy in protein
A
4 cal / g
4
Q
how many cal of energy in lipids
A
9 cal / g
5
Q
a compound that participates in a chemical reaction which produces a compound
A
precursor
6
Q
this is the starting material for heme synthesis
A
glycine
7
Q
this gives the blood the ability to carry oxygen
A
heme
8
Q
precursor for glutathione
A
glycine
9
Q
function of glutathione
A
anti-oxidant
10
Q
precursor for serotonin
A
tryptophan
11
Q
precursor for histamine (allergies)
A
histidine
12
Q
function of amino acids that plays a role in the activation / inactivation of enzymes
A
components of other biologically active constituents
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)
14
Q
This is where the 4 different groups attach
A
second carbon / alpha carbon
14
Q
what do you call a carbon atom that has 4 different subtituents
A
chiral / asymmetric carbon
14
Q
the only amino acid that is not chiral
A
glycine
15
Q
why is glycine not chiral
A
it has two H atoms
16
Q
the two distinguishable isomers
A
L and D Phenylalanine
17
Q
isomer that are found in bacterial cell walls and some antibiotics
A
D-stereoisomers
18
Q
isomer that is oriented to the right side
A
D-Phenylalanine
19
Q
isomer oriented to the left side
A
L-Phenylalanine
20
Q
T or F
The R group determines the structure and function of amino acid molecules
A
F
protein molecules
21
Q
T or F
R group varies in each amino acid, they can be either alcohol or hydrocarbon side chains
A
T
22
Q
This defines the shape of the protein and how they interact with the environment
A
R groups
23
side chains that repel water
nonpolar side chains
24
side chains that love water
polar side chains
25
Are polar side chains in the interior or surfaces of the protein?
surface
26
Are nonpolar side chains in the interior or surfaces of the protein?
interior
27
These are neutral amino acids
nonpolar and polar uncharged (both have no charges)
28
what causes nonpolar amino acids to be hydrophobic
the hydrocarbon molecules (C & H)
29
what are aliphatic R groups made out of
alkyl groups (CH3)
30
This aliphatic r group has no chiral carbon
Gly
31
the only true aliphatic R groups
Ala, Val, Leu, Ile
32
smallest and simplest amino acid
Gly
33
isomer of leucine
isoleucine
34
T or F
the increasing amount of branching in aliphatic R groups are inversely proportional to how hydrophobic it is
F directly proportional (why though, like what does branching have to do with it ??)
35
First amino acid in the sequence
Edit: I think it is also the First amino acid in translation process
methionine
36
cyclic aliphatic R group
proline
37
what do you call the five membered rings in proline
pyrolibine
38
what is the rigidity of the pyrolibine for
protein structure (collagen)
39
What causes Methionine to by hydrophobic
Sulfur
40
Type of nonpolar amino acids that is made up of carbon and hydrogen, and has rings
aromatic R groups
41
nonpolar aromatic r group which is linked to beta carbon
phenyl group (phenol at indole din)
42
what is the phenyl group a substituent of
methylene
43
nonpolar aromatic r group that has an electronegative atom in the ring system
Tryptophan
44
What do you call the ring in tryptophan
indole ring
45
least hydrophobic of the 3 aromatic amino acid side chain
Tyrosine
46
phenylalanine with aromatic OH group (phenolic OH)
Tyrosine
47
most hydrophobic out of the aromatic amino acid side chains
phenylalanine
48
Where does aromatic amino acids absorb light
near the UV region of EM spectrum (250-300 nm)
49
what are the absorbed UV light used for
detection and quantification of proteins
50
Has the highest molar absorptivity
Trp
51
enumerate the lowest to highest molar absorptivity
Phe, Tyr, Trp
52
also absorbs within the UV range but much less than aromatics
disulfide bonds
53
polar groups that have zero net charge or neutral pH
uncharged R groups
54
These are aliphatic OH groups not ionizable in pH range 1-13
Ser and Thr
55
first amino acid discovered
Asparagine
56
Very polar uncharged R groups that cannot be ionized
Ser, Thr, Asn, Gln
57
uncharged r group that is not very polar and can be ionized
Cys
58
the difference between cysteine and serine
cysteine has a thiol group
59
relevant pH range of thiol to lose its proton
pKa of about 8.5 (indi ko din masyado gets ito pero sabi ni madam eh)
60
what is formed by combining two cysteines
cystine
61
amino acids that are strongly polar, found at the exterior surface of the protein
positively charged R groups/polar basic
62
What atom does positively charged R groups contain that accepts protons, making it bear a fully positive charge
nitrogen atom
63
most basic positively charged R group
Arg / guanidino group
64
positively charged r group that is from am ε-amino group (primary amino group)
Lys
65
imidazole functional group (has 2 N atoms in 5-membered unsaturated ring)
His
66
least basic, almost neutral positively charged r group
His
67
Polar amino acids that contains a carboxylic acid (COO-) as part of their side chain
negative charged r groups
68
Found in several proteins including mammalian glutathione peroxidase
selenocysteine
69
what inserts selenocysteine into proteins
UGA
70
The difference between cysteine and selenocysteine
sulfur atom is replaced by selene atom
71
found in monomethylamine methyltransferase
pyrrolysine
72
Where is pyrrolysine from
methanosaricina bakeri (fresh water microbe)
73
What incorporates pyrrolisine in the protein
UAG
74
where is pyrrolisine found
a few archaea and eubacteria, usually in microbes
75
Type of interaction wherein -OH group is binded to a carboxylic group
hydrogen bonding
76
Type of interaction wherein -COOH is bonded to an amino group
ionic interaction
77
Type of interaction between two nonpolar r groups
hydrophobic interaction of nonpolar r groups
78
Type of interaction between two sulfurs
disulfide bonds
79
Form of amino acid wherein both the carboxyl and amino group are neither negative nor positive
unionized form
80
form of amino acid that doesn't exist in the body, for computation purposes only
unionized form
81
form of amino acid that exists in the body
dipolar or zwitterion form
82
what is the charge of the amino group and carboxyl group in dipolar / zwitterion form
Amino group → POSITIVELY CHARGED
Carboxyl group → NEGATIVELY CHARGED
83
This is when equal amounts of positive and negative charge are present at the same time
electrically neutral
84
T or F
charges are directly proportional to solubility
T
85
This means that all hydrogen are attached
fully protonated
86
Charge of amino group in fully protonated pH 1
positive
87
This means that all hydrogen are removed
Fully ionized / Dissociated or Deprotonated pH 11
88
charge of carboxyl and amino group in fully ionized form
Carboxyl group → NEGATIVELY CHARGED
Amino group → Not positively charged
89
the gradual addition or removal of protein
Acid and base titration of amino acids
90
T or F
titration cannot predict the charge of an amino acid in a given solution with a unknown pH
T (kasi need na known yun pH)
91
T or F
At low pH of 1.0 the carboxylic and group is protonated.
T
92
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)
F (loses)
93
T or F
At basic pH, titration causes the amino group to lose its hydrogen
T
94
this is the pH at which the NET charge on a molecule is ZERO
isoelectric point (PI)
95
If pH < pI, what is the net charge
positive
96
If pH > pI, what is the net charge
negative
97
it is computed as the pH exactly halfway between the two pKa values surrounding the zero net charge
PI value
98
the equivalence point on the titration curve
average of pI
99
we need the ____to compute for the isoelectric point whether the amino acid can take up or donate to a proton
pKa
100
is the amino acid protonated or deprotonated when pH solution is less than the pKa?
protonated (+)
101
is the amino acid protonated or deprotonated when pH solution is greater than the pKa?
deprotonated (-)
102
How many pKa's for neutral side chains?
2
103
two pKa's for neutral side chains
1 carboxyl
1 amino group
104
T or F
All amino acids have at least 3 ionizable groups
F 2
105
T or F
pKa1 is the pka of NH3 group
F (COOH)
106
T or F
pKa3 is the pKa of side chain varies (R group)
T
107
T or F
pKa2 is the pKa of NH3 group
T
108
pKa's used for amino acids with acidic side chains
pKa1 and pKa2
109
pKa's used for amino acids with basic side chains
pKa2 and pKa3
110
form that is the most positively charged happens at low ph; pH 1
cationic form
111
form that exists at high pH (12)
ionic form
112
You have reached the end of this week’s flash cards
Hug nath the following day or you and ur family will be cursed for the next 3 generations
113
Type of ring that phenylalanine have
Phenyl ring
114
Type of ring that tyrosine have
Phenol ring
