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Biochemistry > Midterms Lec > Flashcards

Midterms Lec Flashcards

1
Q

came from the Greek word
proteios which means ‘first place’

A

proteins

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2
Q

Most abundant organic
molecule in the human body comprising more than 50% of
the cell’s dry mass

A

protein

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3
Q

Composed of many amino
acids bounded together via the
peptide linkage thus providing
a diverse range of functions

A

protein

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4
Q

function of protein for support,
contraction, and movement

A

structural

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5
Q

the
contractile protein of the
muscles (myocytes

A

actin myosin

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6
Q

component protein
of microtubules

A

tubulin

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7
Q

function of protein that bind and carry
substances from one place to
another

A

transport

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8
Q

the carrier of O2 in the
muscles and blood
respectively

A

myoglobin, hemoglobin

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9
Q

functions of protein that enhance the rate of
biochemical reactions

A

catalyst

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10
Q

speed up the breakdown of
starch

A

amylase

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11
Q

more
commonly known as
antibodies produced by
immune cells (lymphocytes)

A

immunoglobulin

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12
Q

are released into the
bloodstream and regulate the
physiologic activities of their
target cells

A

hormones

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13
Q

produced by β cells
of the pancreas. It lowers the
level of glucose in the blood.

A

insulin

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14
Q

deficiency in
insulin leads to this disease

A

diabetes

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15
Q

function of protein that can be used in metabolic
reactions that yield energy

A

energy source

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16
Q

major protein in
milk

A

casein

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17
Q

protein in egg
white

A

egg albumin

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18
Q

Variation in amino acid is caused by (3)

A

order of amino acid
chain length
folding the chain in distinct ways

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19
Q

about this much protein
should be consumed in the diet

A

14 percent

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20
Q

source of protein include:

A

meat
fish
eggs
peas
beans
nuts

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21
Q

breaks down proteins in
order to be absorbed into the
bloodstream to be assimilated by the
body

A

enzymes

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22
Q

used to test for protein

A

copper sulfate solution
sodium hydroxide

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23
Q

Can be also called Biuret
solution

A

copper sulfate
sodium hydroxide

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24
Q

overall threedimensional
shape of protein

A

native fonrimation

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25
Q

Four hierarchical levels of protein

A

primary
secondary
tertiary
quaternary

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26
Q

The amino acid sequence of
the protein. This is the sole
determinant of its overall
shape

A

primary structure

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27
Q

rule that states the amino acid sequence is the sole determinant of its overall shape

A

Anfinsen’s rule

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28
Q

The first amino acid residue
is written to the left as the _-terminal

A

N

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29
Q

Meanwhile, the __terminal
is always the last
and rightmost amino acid.

A

C

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30
Q

The local folding of protein
segment into helical or
sheet-like structure

A

secondary structure

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31
Q

formed by the
coiling of the polypeptide
chain into a right-handed
spiral

A

alpha-helix

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32
Q

formed
when two adjacent chains of
polypeptides forms H-bonds
in an almost fully extended
form that can be likened to
the pleats of an accordion

A

beta-pleated sheet

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33
Q

The compact threedimensional
structure or
native conformation of
protein

A

tertiary

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34
Q

tertiary structure is stabilized by:

A

H-bonds
Salt bridges
hydrophobic interactions
disulfide bridges

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35
Q

In general, proteins are
either ____or ____in
shape.

A

fibrous
globular

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36
Q

those that
exist as fibers or sheets. They
are made up of one type of
secondary structure and
function for structural
support

A

fibrous proteins

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37
Q

Examples include: collagen,
keratin, and silk fibroin

A

fibrous protein

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38
Q

combinations of different
secondary structures that
compactly folded into
spherical shapes

A

globular protein

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39
Q

Examples include: enzmes,
myoglobin, and hemoglobin

A

globulular protein

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40
Q

Involves the interaction of the
subunits of an oligomeric
protein

A

quaternary

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41
Q

proteins like hemoglobin

A

quaternary structrure

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42
Q

functional group formed
when a peptide bond is made

A

amide

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43
Q

– 3-10 amino acids
combining

A

oligopeptide

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44
Q
  • > 10 amino acids
A

polypeptide

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45
Q

each monomeric unit in the
polypeptide

A

residue

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46
Q

localized conformation of the chain

A

secondary protein structure

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47
Q

peptide bond has this
character due to resonance

A

Pi bond

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48
Q

bonds
formed in the β-pleated sheet

A

dipole dipole interactions

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49
Q

Stores energy, example of a
favorable conformation

A

dipole dipole interactions

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50
Q

spiral shaped with 3.6
residues for turn

A

alpha helix

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51
Q

➢ R groups are pointing out

A

alpha helix

52
Q

Factors that influence tertiary
structure

A

hydrophobic residues
hydrophilic residues

53
Q

through mild
oxidation, two cysteine can react to
form this bond

A

disulfide bond

54
Q

Covalent linkage between two
sulfur atoms

A

disulfide bond

55
Q

sulfur analog of a hydroxyl
group

A

thiol

56
Q

amino acid
residue of Glutamic acid is changed
to Valine

A

sickle cell disease

57
Q

most abundant protein in
the human bod

A

collagen

58
Q

Cementing component of
various connective tissues
like bones, tendons,
ligaments, and skin

A

collagen

59
Q

Made up of three-left handed
helices that are twisted
together to form a righthanded
super helix (likened to
a rope made of three cords)

A

collagen

60
Q

Tough, yet flexible

A

collagen

61
Q

Structure is a repeating
sequence of what

A

Gly-Pro-X

62
Q

X in collagen can be

A

4-hydroxyproline
lysine residue

63
Q

essential
for this hydroxylation and is
therefore critical in maintaining the
structural integrity of collagen

A

ascorbic acid

64
Q

severe deficiency in vitamin
C leads to this, which is
characterized by swelling and
inflammation of gums, impaired
healing of wounds, loosening of
teeth, pain in joints, and progressive
weakening of the body

A

scurvy

65
Q

major fibrous protein
in hair and nails, and a minor
constituent of the skin

A

alpha keratin

66
Q

Component of the cells
cytoskeleton that maintains
their shape

A

alpha keratin

67
Q

Made up of two alpha-helices
that are twisted together to
form a left-handed super helix

A

alpha keratin

68
Q

extensively
stabilize the structure of
keratin

A

disulfide bond

69
Q

in fat, it is the major
protein in the extra cellular matrix

A

collagen

70
Q

Most abundant protein in
vertebrate

A

collagen

71
Q

collagen has two types

A

fibrillar type
non-fibrilar

72
Q

Five most common type of collagens
are:

A

Type I- V

73
Q

type of collagen that is abundant in skin,
tendon, vasculature, organs,
bone (main component of the
organic part of the bone)

A

type I

74
Q

type of collagen that is cartilage (main
collagenous component of
cartilage)

A

type II

75
Q

reticulate (main
component of reticular fibers,
commonly found alongside
type I)

A

type II

76
Q

forms basal lamina,
the epithelium-secreted layer
of the basement membrane

type of collagen

A

type IV collagen

77
Q

, plays an essential role in the health of our hair and cell surfaces. It contributes to the strength and thickness of hair strands, promoting healthy hair growth.

type of collagen

A

type V

78
Q

Has two identical chains (a1)
and additional chain that
differs slightly in its chemical
composition (a2)

A

collagen

79
Q

have 25 different alpha
chains encoded by different genes

A

vertebrates

80
Q

is found at almost
every third residue in collagen

A

glycine

81
Q

makes up about 17
percent of collagen

A

proline

82
Q

can be
derived from proline

A

hydroxyproline

83
Q

depending on the
type of collagen, varying
numbers of hydroxylysines
are ______(mostly
having disaccharides
attached)

A

glycosylated

84
Q

Basic composition is
essentially the same, but
myoglobin is made up of a
____ unit while hemoglobin
has ____subunits

A

single
four

85
Q

nonprotein
component of the subunit

A

prothestic group

86
Q

group in hemoglobin which
consist of a tetrapyrrole ring called
porphyrin with a coordinated Fe2+
atom

A

heme

87
Q

the released
myoglobin is filtered by the kidneys
but is toxic to the renal tubular
epithelium and so may cause acute
kidney injury

A

rhabdomyolysis

87
Q

myoglobin and hemoglobin
bind to this

A

oxygen

88
Q

how many amino acids in myoglobin

A

153

89
Q

how many amino acids in hemoglobin

A

146aa (b)
141aa (a)

90
Q

who has a higher affinity for oxygen?

myo or hemo?

A

myo

91
Q

which is for storage? for transport?

myo or hemo

A

myo - storage
hemo - transport

92
Q

which has distinct structural change

myo or hemo

A

myo

93
Q

constraints between subunits
oppose the structural changes
resulting from ligand binding

A

T state

94
Q

constraints are released in the
subunits, thus enhancing
ligand-binding affinity

A

R state

95
Q

genetic disease
where RBCs can take the shape of a
sickle

A

sickle cell anemia

96
Q

More easily destroyed,
causing anemia

A

sickle cell anemia

97
Q

– made up of
two α-globin and two β-globin

A

hemoglobin A

98
Q

A/B-globin cells end up
misshapen

A

B

99
Q

can carry oxygen, but changes
shape when deoxygenated that can
clump with other sickle hemoglobin

A

HbS

100
Q

decreases Hb
affinity for O2

A

acidosis

101
Q

free hemoglobin is
bounded by this, recycling it

A

haptoglobin

102
Q

low levels of this is a sign of
intravascular hemolysis

A

haptoglobin

103
Q

peptide hormone that is
produced by the beta cells of the
pancreas

A

insulin

104
Q

beta cells of pancreas

A

islets of langerhans

105
Q

dimetric protein made up of Achain
and B-chain which
contains 21 and 30 amino acid
residues respectively

A

insulin

106
Q

has two alpha helical
regions at A1-A8 and A12-A19
which are anti parallel

A

a chain

107
Q

has a central alpha
helical structure from amino
acid B9-B19 which are flanked
by the disulfide bond on either
sides and two beta sheets at
amino acid B7-B10 and B-20
and B-23

A

b chain

108
Q

deficiency in
insulin production or resistance to
insulin results to this, which is a
metabolic disorder that is
characterized by hyperglycemia

A

diabetes mellitus

109
Q

high blood
sugar resulting to serious
health complications like
kidney failure, cardiovascular
disease, stroke, nerve
damage, and eye damage

A

hyperglycemia

110
Q

Symptoms include frequent
urination, increased thirst,
impaired wound healing, and
increased appetite

A

hyperglycemia

111
Q
  • How are proteins formed:
A

replication
transcription
translation

112
Q

large molecules made up
of chains of amino acids

A

proteins

113
Q

all essential
amino acids are present

A

complete proteins

114
Q

food with complete proteins

A

beef
poultry
fish
eggs
soy

115
Q

include nuts,
seed, beans

A

incomplete proteins

116
Q

determines the function
of the protein

A

structure

117
Q

all information
required to specify the structure of a
protein is encoded in this

A

primary structure

118
Q

local folding
of protein segment:

A

secondary structure

119
Q

coiling into right
handed spiral, 10 turns 5.4
nanometers

A

a helix

120
Q

adjacent
polypeptide chains form H
bonds

A

beta pleated sheet

121
Q

3D structure that are
slender, fibers or sheets made up of
1 type of secondary structure

A

fibrous structure

122
Q

3D structure that is
spherical, compact and forms
hydrophilic and hydrophobic regions

A

globular

123
Q

Made up of different
secondary structures

A

globular

124
Q

oxidation reaction in
which carbon-hydrogen bond
oxidizes to carbon-hydroxyl

A

hydroxylation

Biochemistry (12 decks)

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