Proteins Flashcards
1
Q
Building blocks of proteins?
A
amino acids
2
Q
T or F- there are 30 amino acid and 11 are essential.
A
F- There is only 20 amino acids and 9 are essential
3
Q
disruption of tertiary structure in a protein?
A
Denaturation
4
Q
T or F - there are 2 types of denaturation : reversible and irreversible
A
T
5
Q
Normal Range of pH Level?
A
7.35-7.45
6
Q
Normal Range of pCo2?
A
35-45mmHg
7
Q
Normal Range of HCO3?
A
19-24meq/L
8
Q
Formula of Henderson Hasselbach?
A
pH= pka+ log of HCO3/CO2
9
Q
T or F- is protein an enzyme?
A
T
10
Q
has amino group and carboxylic group?
A
Amino Acid
11
Q
molecules that combine to form proteins
A
Amino Acid
12
Q
How many essential amino acid and what are those?
A
9 H-istidine I-soleucine L-eucine L-ysine M-ethoinine P-henyalanine T-yrpthophan T-hreonine V-aline
13
Q
T or F- Non Polar amino acids are hydrophilic
A
F- Non Polar are hydrophobic - water fearing
14
Q
T of F- cation is (+) charge anion is (-) charge
if these are migrated to:
cation->cathode it becomes (-) charge
anion->anode it becomes (+) charge
A
T
15
Q
the weakest intermolecular force?
A
London dispertion
16
Q
forces in non polar aa?
A
London forces and Van der Waals forces
17
Q
forces in basic aa?
A
salt bridges
18
Q
forces in aromatic aa?
A
pi-pi complex (benzene rings)
19
Q
forces in acidic aa?
A
salt bridges
20
Q
forces in polar neutral?
A
h-bond
21
Q
what is the electrical charge of polar neutral?
A
0
22
Q
electrical charge of acidic?
A
negative (-)
23
Q
electrical charge of basic?
A
positive (+)
24
Q
how many Nonpolar aa and what are those?
A
7 G-lycine A-lanine P-roline V-aline L-eucine I-soleucine M-ethoinine
25
what is K in proteins?
Lysine (3 letter: Lys)
26
What is D in proteins?
Asparatic Acid (3 letter: Asd)
27
how many Aromatic aa and what are those?
3
F- Phenylalanine (3 letter: Phe)
Y- Tyrosine (3 letter: Tyr)
W- Tryptophan (3 letter: Trp)
28
proteins that we can find in milk?
tryptophan
29
Artificial sweetener?
Aspartame
30
halfway between 2 pka?
Isoelectric point ( 0 net charge)
31
MAIN MACHINERIES of organisms?
Protein (found in milk, eggs, meat, fish)
32
pH level is LOW
Protonation
33
plays a critical role, they do most of the work in cell in the body?
Protein
34
pH>pka : proton acceptor?
Deprotonation
35
What formula is this?
| pka1+pka2/2
neutral & acidic
36
when added to a base it acts as weak acid or conjugate base ?
Buffer
37
T or F- when net charge is 0 the protein is soluble
F- under 0 net charge proteins PRECIPITATES
38
Isoelectric pH?
6
39
2 ionizable H+ ions: –NH3 + and –COOH groups; R group/side chain is uncharged
Diprotic (found in neutral aa)
40
```
pH range where an amino acid exhibits its
buffer action (+/- 1pH unit from the given pKa value) against added acid/base to keep the pH of the solution
nearly constant.
```
Buffer region
41
what is protein Q?
Glutamine ( 3letter: Gln)
42
protein with sulfur attached to aliphatic hydrocarbons
methionine
43
helix breaker
proline
44
-SH
Thiol Group
45
S-S
Disulfide Bond
46
responsible of permanent perm?
```
thiol group (-SH)
-it can break the S-S bonds
```
47
protein with sulfur and is used in lead acetate test?
```
C Cysteine (3 letter: Cys)
it has thiol
```
48
with extra carboxylic group in the side chains?
Acidic AA
49
with extra amino group in the side chains?
Basic AA
50
AA _______ the ability to act either
as a weak Bronsted acid/ base or a conjugate acid-base pair as the
pH of the solution changes.
Amphoteric Property
51
T or F - amino acid and proteins can serve as buffers in body fluids
T
52
greater than zero. precipitate or soluble?
Soluble
53
T or F- pH under alkalosis will have a -1 net charge
T
54
chain of 2 amino acid?
peptide/amide bonds
55
chain of many amino acid?
polypeptide
56
T or F - pH under acidosis will have a +1 net charge
T
57
movement of charges contributes to the ABILITY OF PROTEINS TO BE SOLUBLE?
Isoelectric point (PI)
58
T or F-
Above or Below PI: either will REPULSE or ATTRACT
-Proteins are soluble too
T
59
method of
separating and purifying protein molecules and amino acids using an
electric current.
Electrophoresis
60
no migration, zero charge
Zwitterion
61
T or F
| amino acid/protein share the same isoelectric point
F- aa and proteins has its own isoelectric point
62
T or F
| adding a strong acid or base greatly alters its solubility.
T- kasi pag naging 0 charge it will precipitate.
| pag ><0 it is soluble
63
shift in the position of a pair of electrons shared
| between two atoms
Peptide or Amide Bonds
64
protein folding occurs in?
tertiary structure
65
T or F
| protein denaturation is so strong that it could actually destroy the primary, secondary, tertiary, quaternary structure.
F- denaturation is only weak disruption. it can't dissolve the primary structure
66
no free rotation around the peptide bond
stereochemical constraint
67
T or F
| in the formation of peptide bonds dehydration happens
T - (OH) will be removed from the carboxylic group of the other protein and (H) will be removed from the amino group of the other protein
H20 is released therefore it is Dehydration
68
stimulates uterine contractions during labor, lactation
| aka LOVE HORMONE
Oxytocin
69
regulates blood pressure, antidiuretic.
behavior of being territoriality, aggression, and social group defense
among males
Vasopressin
70
Primary Structure consist of?
Peptide bonds
71
2 Denaturing agents?
Physical- heat, friction, UV, ultrasound, High pressure
| Chemical- acid, alkalis, heavy metals, salt, ethanol, urea
72
disruption of weak linkages or bonds
Protein denaturation
73
Secondary Structure consist of?
a-helix and b-pleated sheets
74
two AA link together
dipeptide
75
three AA link together
tripeptide
76
gene mutation: single change in the AA building blocks of
hemoglobin.
HbS tend to stick together and form rigid molecules
- (a crescent-like, “sickle-cell” shape)
Sickle Cell Disease
77
proteins that does not have alpha amino group
| "helix breaker"
Proline
78
T or F- Collagen are triple helix
T
79
most abundant protein found in
bones and connective tissues.
water-insoluble fiber of great strength
Collagen ( paa ng manok rich in collagen kaya nakakaputi)
80
co-factor of a hydroxylating enzyme
Vit C
81
vitamin C deficiency due to malnutrition
Scurvy
82
h-bond is formed in between segments ==== of polypeptide chain
could be parallel or anti-parallel
b-pleated sheet
83
intramolecular H bond parallel to its helix
a-helix
84
normal plasma proteins found in highest concentration in the CNS
Prions
85
(proteinaceous infectious particles) happen when
α-helix folds into a beta sheet that leads to incorrect folding in the
tertiary structure
Aberrant Prions - spongy appearance of the brain
86
T or F BSE affects the CNS, leads to death of the brain’s nerve cells and CAN'T
be fatal
F - Bovine Spongiform Encephalopathy is FATAL
87
conformations of the side chains and the positions of any metal prosthetic
groups.
formation of a-helix and b-pleated sheet with one another
Tertiary Structure
88
Noncovalent Forces are?
Van der Waals
H-bond
Salt Bridge
Pi-pi complex
89
Covalent Forces
S-S (disulfide bonds)
90
single polypeptide chain, 153 AA
| - eight α-helices and no β-pleated sheets
myoglobin
91
shape of the hair follicle and presence of disulfide bonds determine hair’s
genetic trait
Keratin
92
what causes a curve in the hair?
strong covalent S-S bonds
the more disulfide bonds the curvier the hair
93
T or F
| temporary perm includes heat and moisture to disrupt weak forces in hair
T
94
oxidizing agent to convert –SH
| group into new S-S disulfide bonds
Dehydrogenation Reaction
95
thiol (‐SH) acts a reducing agent
and breaks the S-S bonds to
produce Cysteine, -SH
Hydrogenation Reaction
96
```
keratin molecules are now free to
move and adjust to the shape of the
curling rods
keratin molecules are now locked
into the shape of the curls
```
Permanent Perm
97
these are the subunits
| more than one polypeptide chain
Quaternary Structure
98
two alpha and beta subunits
tetramer
| ex is HEMOGLOBIN
99
changes in one site of a protein molecule may cause
| changes in properties at a distant site
Allosteric
100
when one subunit binds, it becomes easier
| for the next subunit to bind
Positive Cooperativy
101
-effect of H+ ion on hemoglobin’s affinity for oxygen (myoglobin is
not affected)
- improves O2 delivery in metabolically active tissues
- high skeletal muscle activity
Bohr effect
102
presence of BPG decreases the hemoglobin’s affinity for O2
BPG (Biphosphoglycerate)
103
T or F
fetal hemoglobin binds less strongly to BPG than maternal hemoglobin
it ensures growing fetus with O2 from mother’s bloodstream through the
placenta
T
104
long and narrow rod
| helical backbone does not fold back, only the side chains
Fibrous Proteins
105
helical and pleated sheets fold back on each other
| interactions between side chains determine protein folding
Globular Proteins
106
unfolding of a protein or disruption of the tertiary structure
Protein Denaturation
107
T or F
| denatured proteins are functional
F- non-functional na kasi na unfold yung structures
108
4 types of protein hydrolysis?
Trypsin
Chymotrypsin
Aminopeptidase
Carboxypeptidase
109
cleaves the 1st amino acid in the polypeptide chain
Aminopeptidase
110
cleaves peptides with basic amino acids at C-terminal
Trypsin
111
cleaves the last amino acid in the polypeptide chain
Carboxypeptidase
112
- cleaves peptides with aromatic amino acids at C-terminal
Chymotrypsin
113
highly resistant to UV rays incorrect folding of tertiary structure
Bovine Spongiform Encephalophaty
