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MAJOR!!! > protein > Flashcards

protein Flashcards

1
Q

Peptides and proteins are formed when amino acids are joined together by

A

amide bonds

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2
Q

has two amino acids joined together by one amide bond

A

dipeptide

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3
Q

The amide bond is called a

A

peptide bond

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4
Q

have many amino acids, while proteins is usually reserved for polymers of > 40 amino acids.

A

Polypeptides

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5
Q

The amino acid with the free –NH3+ group is the N-terminal amino acid and is written on the?

A

left

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6
Q

The amino acid with the free –COO− group is the C-terminal amino acid and is written on the?

A

right

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7
Q

pentapeptides synthesized in the brain act as pain killers and sedatives by binding to pain receptors

A

Enkephalins

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8
Q

Enkephalins has two types

A

Met- enkephalin and leu-enkephalin

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9
Q

contains amino acid that blocks pain and are thought to produce the feeling of well being experienced by an athlete after excessive or strenuous exercise

A

Endorphins

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10
Q

are cyclic nonapeptide hormones secreted by the pituitary gland. They are identical in structure except for two amino acids

A

Oxytocin and Vasopressin

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11
Q

Biological Functions of Proteins

A

Enzymatic catalysis
Transport Proteins
Nutrient Proteins
Storage Proteins
Contractile Proteins
Structural Proteins (Collagen, Elastin, Keratin, Fibrin)
Defense Proteins (Antibodies, Prothrombin and
fibrinogen)
Regulatory Proteins

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12
Q

Simple Proteins

A

Albumin
Globulins
Glutelins
Prolamines
Scleroproteins of Albuminoids
Histones
Protamines

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13
Q

regulate ADH

A

vasopressin

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14
Q

enzymes in lactation

A

oxytocin

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15
Q

Conjugated Proteins

A

Nucleoproteins
Glycoproteins and mucoproteins
Phosphoteins
Chromoproteins
Lipoproteins
Metalloproteins

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16
Q

for clot formation

A

fibrin

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17
Q

part of clotting

A

prothrombin

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18
Q

produce by plasma cells

A

antibodies

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19
Q

transport nutrition

A

albumin

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20
Q

regulates cholesterol

A

lipoproteins

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21
Q

Proteins
Metaproteins
Coagulate Proteins

A

Primary Derived Proteins

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22
Q

Proteases
Peptones
Peptines

A

Secondarily derived Proteins

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23
Q

The ____ of a protein is the sequence of amino acids joined together by peptide bonds

A

primary structure

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24
Q

is the 3D arrangement of localized regions of a
protein.

A

secondary structure

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25
Q

These regions arise due to hydrogen bonding between the N—H group
of one amide with the C═O group of another

A

Secondary Structure

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26
Q

is the 3D shape adopted by the entire peptide chain

A

tertiary structure

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27
Q

Maximize Hydrogen bonding with water (hydrophilic)

A

tertiary structure

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28
Q

Stabilize non-polar sidechains by london dispersion forces
(hydrophobic)

A

tertiary structure

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29
Q

Polar functional groups H-bond with each other

A

tertiary structure

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30
Q

Charged sidechains attracted through electrostatic interactions and disulfide bonds form

A

tertiary structure

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31
Q

The ____ of the protein is the shape adopted when two or more folded poly-peptide chains come together into one complex

A

quaternary structure

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32
Q

bad cholesterol

A

LOW DENSITY LIPOPROTEIN

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33
Q

GOOD CHOLESTEROL

A

HIGH DENSITY LIPOPROTEIN

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34
Q

part of hemoglobin metabolism that toxic in body

A

billirubin

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35
Q

cause by a yellowish in skin

A

billirubin

36
Q

billi in blood

A

jaundice

37
Q

Bonds Responsible for Protein Structure

A

Peptide Bonds
Disulfide Bonds
Hydrogen Bonds
Hydrophobic Bonds
Electrostatic or ionic bonds

38
Q

involves breaking the peptide bonds by treatment with aqueous acid, base, or certain enzymes

A

Protein hydrolysis

39
Q

the process of altering the shape of a protein without breaking the amide bonds that form the primary structure: heat, acid, base, or agitation

A

Denaturation

40
Q

Physical agents

A

Heat
Surface Tension
UV light
High Pressure

41
Q

Chemical agents

A

Organic Solvent
1. Acids and Alkalines
2. Urea and guanidine
Detergents

42
Q

Decreased solubility at the protein’s isoelectric point

A

Chemical Alterations brought about by denaturation

43
Q

As a result of the unfolding process in denaturation, many chemical groups which were rather inactive awing be shielding of the native state become exposed and more readily detectable

A

Chemical Alterations brought about by denaturation

44
Q

Increases in the viscosity of the solution, so the rate of diffusion of the protein molecules decrease

A

Physical Alterations brought about by denaturation

45
Q

Increase levorotation

A

Physical Alterations brought about by denaturation

46
Q

Denatured proteins cannot be crystallized since the formation of a crystal depends upon a high degree of organization of the molecules

A

Physical Alterations brought about by denaturation

47
Q

Increased digestibility by proteolytic enzyme

A

Biological Alterations brought about by denaturation

48
Q

Enzymatic or hormonal activity is usually destroyed

A

Biological Alterations brought about by denaturation

49
Q

The antigenic or antibody functions of proteins are frequently altered as well

A

Biological Alterations brought about by denaturation

50
Q

composed of long linear polypeptide chains that are bundled together to form rods or sheets. Insoluble and serve structural roles giving strength and protection to tissues

A

Fibrous proteins

51
Q

are coiled into compact shapes with hydrophilic outer surfaces that make them water soluble. Enzymes and transport proteins are globular to make them soluble in blood and other aqueous environments

A

Globular proteins

52
Q

These are proteins found in hair, hooves, nails, skin, and wool
having large numbers of alanine and leucine residues

A

α-Keratins

53
Q

Insoluble in water since the polar amino acids extend outward of the alpha helix

A

α-Keratins

54
Q

Two α-Keratins coil around each other, forming a structure called a

A

supercoil or superhelix

55
Q

Most abundant protein in vertebrates, found in the connective tissues such as bones, cartilage, tendons, teeth and blood vessels

A

collagen

56
Q

Glycine and proline account large fraction of its amino acid residues

A

collagen

57
Q

forms an elongated left-handed helix

A

collagen

58
Q

three of theses helices wind wound each other to form right handed

A

superhelix or triple helix

59
Q

are proteins that serve as biological catalysts for reactions in all living organisms

A

enzymes

60
Q

need for action to occur

A

catalyst

61
Q

They increase the rate of a reaction (10^6 to 10^12 times faster), but are unchanged themselves.

A

enzymes

62
Q

very specific; each of these catalyzes a certain reaction or type of reaction only

A

enzymes

63
Q

The names of most enzymes end with the suffix

A

ase

64
Q

a metal ion or an organic molecule needed for an enzyme-catalyzed reaction to occur

A

cofactor

65
Q

It is a non-protein chemical that is bound to an enzyme and is required for catalysis

A

cofactor

66
Q

2 types of cofactor

A

Coenzyme
Prosthetic Groups

67
Q

enzymes involved in the transfer of electrons; they catalyze reactions involving removal of electrons from an electron donor and transfer them to an appropriate electron. Usually these reactions lead to the formation of ATP

A

Oxidoreductase

68
Q

involved in transferring functional groups between donors and acceptors. Transfer of chemical groups other than hydrogen from one substrate to another

A

transferase

69
Q

cause hydrolysis or splitting of a bond by the addition of
water

A

hydrolase

70
Q

Catalyze the removal of groups from substrates without hydrolysis. The product contains double bond

A

Lyases

71
Q

Catalyzes the interconversion of optical geometric or positional isomers

A

Isomerases

72
Q

Involved in the synthetic reactions when two molecules are joined at the expense of an ATP “high energy phosphate bond”. Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bonding ATP or similar compounds

A

Ligases

73
Q

enzymes reacting

A

b. substrate

74
Q

can bind to enzyme to form an enzyme substrate complex

A

substrate

75
Q

made of long chain of amino acid and the chain are folded to form active site

A

enzymes

76
Q

Extreme pH level may denature enzyme or influence its ionic state resulting in structural change

A

pH

77
Q

the faster the reaction, because more enzyme is present to bind with the substrate

A

the higher the enzyme concentration

78
Q

With the amount of enzyme exceeding the amount of substrate, the reaction rate steadily increases as more substrate is added.

A

Substrate Concentration

79
Q

The ___ an enzyme is incubated with its substrate, the greater the amount of product that will be formed

A

longer

80
Q

the reaction rate depends only on the enzyme concentration

A

Zero- order reaction

81
Q

the reaction rate is directly proportional to substrate concentration

A

First – order reaction

82
Q

is a molecule that causes an enzyme to lose activity

A

inhibitor

83
Q

binds to an enzyme but then enzyme activity is restored when the inhibitor is released

A

Reversible inhibitor

84
Q

has a shape and structure similar to substrate so it competes with the substrate for binding to active site

A

Competitive inhibitor

85
Q

binds to the enzyme but does not bind at the active site

A

Non-Competitive inhibitors

86
Q

Covalently binds ton an enzyme, permanently destroying its activity

A

Irreversible inhibitors

87
Q

inactive type that dissolve the clot

A

plasiminogen

MAJOR!!! (12 decks)

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