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Biochemistry Lecture and Laboratory > Proteins > Flashcards

Proteins Flashcards

1
Q

Building blocks of proteins?

A

amino acids

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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

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3
Q

disruption of tertiary structure in a protein?

A

Denaturation

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4
Q

T or F - there are 2 types of denaturation : reversible and irreversible

A

T

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5
Q

Normal Range of pH Level?

A

7.35-7.45

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6
Q

Normal Range of pCo2?

A

35-45mmHg

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7
Q

Normal Range of HCO3?

A

19-24meq/L

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8
Q

Formula of Henderson Hasselbach?

A

pH= pka+ log of HCO3/CO2

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9
Q

T or F- is protein an enzyme?

A

T

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10
Q

has amino group and carboxylic group?

A

Amino Acid

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11
Q

molecules that combine to form proteins

A

Amino Acid

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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
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13
Q

T or F- Non Polar amino acids are hydrophilic

A

F- Non Polar are hydrophobic - water fearing

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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

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15
Q

the weakest intermolecular force?

A

London dispertion

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16
Q

forces in non polar aa?

A

London forces and Van der Waals forces

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17
Q

forces in basic aa?

A

salt bridges

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18
Q

forces in aromatic aa?

A

pi-pi complex (benzene rings)

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19
Q

forces in acidic aa?

A

salt bridges

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20
Q

forces in polar neutral?

A

h-bond

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21
Q

what is the electrical charge of polar neutral?

A

0

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22
Q

electrical charge of acidic?

A

negative (-)

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23
Q

electrical charge of basic?

A

positive (+)

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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
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25
Q

what is K in proteins?

A

Lysine (3 letter: Lys)

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26
Q

What is D in proteins?

A

Asparatic Acid (3 letter: Asd)

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27
Q

how many Aromatic aa and what are those?

A

3
F- Phenylalanine (3 letter: Phe)
Y- Tyrosine (3 letter: Tyr)
W- Tryptophan (3 letter: Trp)

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28
Q

proteins that we can find in milk?

A

tryptophan

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29
Q

Artificial sweetener?

A

Aspartame

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30
Q

halfway between 2 pka?

A

Isoelectric point ( 0 net charge)

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31
Q

MAIN MACHINERIES of organisms?

A

Protein (found in milk, eggs, meat, fish)

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32
Q

pH level is LOW

A

Protonation

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33
Q

plays a critical role, they do most of the work in cell in the body?

A

Protein

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34
Q

pH>pka : proton acceptor?

A

Deprotonation

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35
Q

What formula is this?

pka1+pka2/2

A

neutral & acidic

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36
Q

when added to a base it acts as weak acid or conjugate base ?

A

Buffer

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37
Q

T or F- when net charge is 0 the protein is soluble

A

F- under 0 net charge proteins PRECIPITATES

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38
Q

Isoelectric pH?

A

6

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39
Q

2 ionizable H+ ions: –NH3 + and –COOH groups; R group/side chain is uncharged

A

Diprotic (found in neutral aa)

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40
Q 
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.
A

Buffer region

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41
Q

what is protein Q?

A

Glutamine ( 3letter: Gln)

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42
Q

protein with sulfur attached to aliphatic hydrocarbons

A

methionine

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43
Q

helix breaker

A

proline

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44
Q

-SH

A

Thiol Group

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45
Q

S-S

A

Disulfide Bond

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46
Q

responsible of permanent perm?

A 
thiol group (-SH) 
-it can break the S-S bonds
47
Q

protein with sulfur and is used in lead acetate test?

A 
C Cysteine (3 letter: Cys)
it has thiol
48
Q

with extra carboxylic group in the side chains?

A

Acidic AA

49
Q

with extra amino group in the side chains?

A

Basic AA

50
Q

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.

A

Amphoteric Property

51
Q

T or F - amino acid and proteins can serve as buffers in body fluids

A

T

52
Q

greater than zero. precipitate or soluble?

A

Soluble

53
Q

T or F- pH under alkalosis will have a -1 net charge

A

T

54
Q

chain of 2 amino acid?

A

peptide/amide bonds

55
Q

chain of many amino acid?

A

polypeptide

56
Q

T or F - pH under acidosis will have a +1 net charge

A

T

57
Q

movement of charges contributes to the ABILITY OF PROTEINS TO BE SOLUBLE?

A

Isoelectric point (PI)

58
Q

T or F-
Above or Below PI: either will REPULSE or ATTRACT
-Proteins are soluble too

A

T

59
Q

method of
separating and purifying protein molecules and amino acids using an
electric current.

A

Electrophoresis

60
Q

no migration, zero charge

A

Zwitterion

61
Q

T or F

amino acid/protein share the same isoelectric point

A

F- aa and proteins has its own isoelectric point

62
Q

T or F

adding a strong acid or base greatly alters its solubility.

A

T- kasi pag naging 0 charge it will precipitate.

pag ><0 it is soluble

63
Q

shift in the position of a pair of electrons shared

between two atoms

A

Peptide or Amide Bonds

64
Q

protein folding occurs in?

A

tertiary structure

65
Q

T or F

protein denaturation is so strong that it could actually destroy the primary, secondary, tertiary, quaternary structure.

A

F- denaturation is only weak disruption. it can’t dissolve the primary structure

66
Q

no free rotation around the peptide bond

A

stereochemical constraint

67
Q

T or F

in the formation of peptide bonds dehydration happens

A

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
Q

stimulates uterine contractions during labor, lactation

aka LOVE HORMONE

A

Oxytocin

69
Q

regulates blood pressure, antidiuretic.
behavior of being territoriality, aggression, and social group defense
among males

A

Vasopressin

70
Q

Primary Structure consist of?

A

Peptide bonds

71
Q

2 Denaturing agents?

A

Physical- heat, friction, UV, ultrasound, High pressure

Chemical- acid, alkalis, heavy metals, salt, ethanol, urea

72
Q

disruption of weak linkages or bonds

A

Protein denaturation

73
Q

Secondary Structure consist of?

A

a-helix and b-pleated sheets

74
Q

two AA link together

A

dipeptide

75
Q

three AA link together

A

tripeptide

76
Q

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)

A

Sickle Cell Disease

77
Q

proteins that does not have alpha amino group

“helix breaker”

A

Proline

78
Q

T or F- Collagen are triple helix

A

T

79
Q

most abundant protein found in
bones and connective tissues.
water-insoluble fiber of great strength

A

Collagen ( paa ng manok rich in collagen kaya nakakaputi)

80
Q

co-factor of a hydroxylating enzyme

A

Vit C

81
Q

vitamin C deficiency due to malnutrition

A

Scurvy

82
Q

h-bond is formed in between segments ==== of polypeptide chain
could be parallel or anti-parallel

A

b-pleated sheet

83
Q

intramolecular H bond parallel to its helix

A

a-helix

84
Q

normal plasma proteins found in highest concentration in the CNS

A

Prions

85
Q

(proteinaceous infectious particles) happen when
α-helix folds into a beta sheet that leads to incorrect folding in the
tertiary structure

A

Aberrant Prions - spongy appearance of the brain

86
Q

T or F BSE affects the CNS, leads to death of the brain’s nerve cells and CAN’T
be fatal

A

F - Bovine Spongiform Encephalopathy is FATAL

87
Q

conformations of the side chains and the positions of any metal prosthetic
groups.
formation of a-helix and b-pleated sheet with one another

A

Tertiary Structure

88
Q

Noncovalent Forces are?

A

Van der Waals
H-bond
Salt Bridge
Pi-pi complex

89
Q

Covalent Forces

A

S-S (disulfide bonds)

90
Q

single polypeptide chain, 153 AA

- eight α-helices and no β-pleated sheets

A

myoglobin

91
Q

shape of the hair follicle and presence of disulfide bonds determine hair’s
genetic trait

A

Keratin

92
Q

what causes a curve in the hair?

A

strong covalent S-S bonds

the more disulfide bonds the curvier the hair

93
Q

T or F

temporary perm includes heat and moisture to disrupt weak forces in hair

A

T

94
Q

oxidizing agent to convert –SH

group into new S-S disulfide bonds

A

Dehydrogenation Reaction

95
Q

thiol (‐SH) acts a reducing agent
and breaks the S-S bonds to
produce Cysteine, -SH

A

Hydrogenation Reaction

96
Q 
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
A

Permanent Perm

97
Q

these are the subunits

more than one polypeptide chain

A

Quaternary Structure

98
Q

two alpha and beta subunits

A

tetramer

ex is HEMOGLOBIN

99
Q

changes in one site of a protein molecule may cause

changes in properties at a distant site

A

Allosteric

100
Q

when one subunit binds, it becomes easier

for the next subunit to bind

A

Positive Cooperativy

101
Q

-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

A

Bohr effect

102
Q

presence of BPG decreases the hemoglobin’s affinity for O2

A

BPG (Biphosphoglycerate)

103
Q

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

A

T

104
Q

long and narrow rod

helical backbone does not fold back, only the side chains

A

Fibrous Proteins

105
Q

helical and pleated sheets fold back on each other

interactions between side chains determine protein folding

A

Globular Proteins

106
Q

unfolding of a protein or disruption of the tertiary structure

A

Protein Denaturation

107
Q

T or F

denatured proteins are functional

A

F- non-functional na kasi na unfold yung structures

108
Q

4 types of protein hydrolysis?

A

Trypsin
Chymotrypsin
Aminopeptidase
Carboxypeptidase

109
Q

cleaves the 1st amino acid in the polypeptide chain

A

Aminopeptidase

110
Q

cleaves peptides with basic amino acids at C-terminal

A

Trypsin

111
Q

cleaves the last amino acid in the polypeptide chain

A

Carboxypeptidase

112
Q
  • cleaves peptides with aromatic amino acids at C-terminal
A

Chymotrypsin

113
Q

highly resistant to UV rays incorrect folding of tertiary structure

A

Bovine Spongiform Encephalophaty

Biochemistry Lecture and Laboratory (8 decks)

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