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Chem 2 > Unit 7 > Flashcards

Unit 7 Flashcards

1
Q

Collagen can be classified as a ______ protein

A

_structural_______

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2
Q

Proteins that stimulate immune response are known as

A

immunoglobin

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3
Q

Amino acids that are not synthesized in the body but must be ingested with the diet are called ________ amino acids.

A

essential

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4
Q

A zwitterion of any amino acid has a net charge of

A

zero

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5
Q

The isoelectric point for any amino acid is the pH at which the amino acid has a net charge of

A

zero

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6
Q

hemoglobin is a

A

quaternary transport protien

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7
Q

1) The protein folds into a compact structure stabilized by interactions between R groups

A

tertiary

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8
Q

2) the combination of two or more protein molecules to form an active protein

A

quaternary

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9
Q

3) pleated sheet

A

secondary

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10
Q

4) the peptide bonds between the amino acids

A

primary structure

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11
Q

5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino acid and the amino group of a different amino acid

A

secondary

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12
Q

list all essential amino acids

A

1) Tryptophan
2) Lysine
3) Methionine
4) Phenylalanine
5) Threonine
6) Valine
7) Leucine
8) Isoleucine

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13
Q

essential amino acid for kids

A

histadine and arginine

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14
Q

Lysine

abbreviation

A

Lys, K

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15
Q

Argine Abrev

A

Arg, R

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16
Q

Methionine Abrev

A

Met, M

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17
Q

Tyrosine Abrev

A

Tyr, Y

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18
Q

Glycine Abrev

A

Gly, G

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19
Q

Alanine Abrev

A

Ala, A

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20
Q

Valine Abrev

A

Val, V

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21
Q

Leucine Abrev

A

Leu, L

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22
Q

Isoleucine Abrev

A

Ile, I

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23
Q

Phenylaline Abrev

A

Phe, F

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24
Q

Methionine Abrev

A

Met, M

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25
Q

Proline Abrev

A

Pro, P

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26
Q

Tryptophan Abrev

A

Trp, W

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27
Q

Serine Abrev

A

Ser, S

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28
Q

Theronine Abrev

A

Thr, T

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29
Q

Tyrosine Abrev

A

Tyr, Y

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30
Q

Cysteine Abrev

A

Cys, C

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31
Q

Asparagine Abrev

A

Asn, N

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32
Q

Aspartate Abrev

A

Asp, D

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33
Q

Glutamine Abrev

A

Gln, Q

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34
Q

Glutamate Abrev

A

Glu, E

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35
Q

Histidine Abrev

A

His, H

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36
Q

Lysine Abrev

A

Lys, K

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37
Q

Arginine Abrev

A

Arg, R

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38
Q

endings changed

A

ine or ate to ly

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39
Q

How many different amino acids are present in proteins?

A

20

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40
Q

Proteins are said to be polymers. True/ False

A

True. A protein is a polymer constructed from a set of monomers called amino acids.

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41
Q

Explain the general structure of an amino acid. Give an example.

A

central C atom (alpha) which is attached to NH2 group, COOH group, H atom and “R”.

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42
Q

Define peptide bond.

A

The amide bond formed when amino acids combine through condensation reaction is known as a peptide bond.

A peptide bond (amide bond) is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain

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43
Q
  1. List the types of protein.
A

1) Enzyme
2) Hormones
3) Storage
4) Transport
5) Contractile
6) Structure
7) Immunity

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44
Q

2 transport proteins

A

hemoglobin

cytochromes

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45
Q

2 hormone proteins

A

insulin

renin

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46
Q

2 structure proteins

A

collagen

keratin

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47
Q

2 immunity proteins

A

immunoglobulins

interleukin 4

48
Q

2 storage proteins

A

ferritin

casein

49
Q

a. the sequence of amino acids held by covalent peptide bonds, which is unique for each protein.

A

primary structure

50
Q

a. When amino acids form H bonds between atoms and within chains constitute this structure. 2 main types are alpha and beta form. In an alpha helix the amino acids are arranged in a right-handed helical form.

A

secondary structure

51
Q

a. The protein folds into a compact structure stabilized by interactions between R groups in this structure. Attractions and repulsions between amino acid residues in polypeptide chain lead to this structure. Most proteins require 2 or more tertiary structures to be biologically active.

A

tertiary structure

52
Q

what are the two interactions involved in tertiary structure

A

hydrophilic

hydrophobic

53
Q

interactions between external aqueous environment and polar amino acid residues. (remnants of amino acids during the formation of peptide bonds are called residues)

A

hydrophilic

54
Q

interactions lead to the formation of a nonpolar region in the center of protein molecule and repelled by hydrophilic interactions.

A

hydrophobic

55
Q

ionic attractions between charges of acidic and basic amino acid residues.

A

salt bridges

56
Q

bonds formed between H and O or N.

A

hydrogen bonds

57
Q

are covalent bonds formed when SH groups are oxidized.

A

disulfide bonds

58
Q

a. The combination of two or more protein molecules to form an active protein takes place in this structure

A

quaternary structure

59
Q

Combination of 2 or more protein polypeptide chains stabilized by the interactions (discussed in tertiary) constitute this structure. Amino acids with different sequences of alpha and beta chains form similar tertiary structures

A

quaternary structure

60
Q

Formed within the same protein chain. Hydrogen bonding can occur between the α-carboxyl group of one residue and the –NH group of its neighbor four units down the same chain. The helical structure can be easily disturbed since hydrogen bond is unstable.

A

alpha helix

61
Q

within the same protein molecule consists of two or more amino acid sequences that are arranged adjacently and in parallel, but with alternating orientation. Thus hydrogen bonds can form between the two strands. Hydrogen bonds established between the N-H groups in the backbone of one strand with the C=O groups in the backbone of the adjacent, parallel strand(s). The sheet’s stability and structural rigidity and integrity are the result of multiple such hydrogen bonds arranged in this way.

A

beta pleated sheet

62
Q

Which are the protein structures affected by denaturation?

A

Denaturing disrupts the secondary, tertiary, or quaternary structure of a protein.

63
Q

Acids and bases denature a protein by

A

disrupting ionic bonds and hydrogen bonds

64
Q

An acid can denature a protein by

A

disrupting hydrogen bonds between R group chains.

65
Q

Heat denatures a protein by

A

disrupting hydrophobic bonds and hydrogen bonds.

66
Q

Heavy metals denature proteins by

A

disrupting disulfide bonds

67
Q

One heavy metal that can cause denaturation of a protein is

A

silver

68
Q

What are active sites? Where are they found?

A

The area where the substrates are held are called active sites, found within the enzyme’s tertiary structure.

69
Q

what happens within active sites

A

residues of amino acids react with functional groups of substrate to form H bonds, salt bridges and hydrophobic interactions.

70
Q

Combination of an enzyme and a substrate within the active site forms an

A

enzyme-substrate complex (ES) that catalyzes the reaction with lower activation energy

71
Q

R groups on amino acid residues does what

A

catalyze the reaction to form enzyme-product complex.

72
Q

(EP) Then the products are

A

released from the molecule so that it binds with another substrate.

73
Q

Rate of enzyme-catalyzed reactions are affected by change in

A

temperature, pH, enzyme and substrate concentration.

74
Q

Inhibitors decrease enzyme activity by

A

binding in active site (competitive inhibition) or at another site on the enzyme (noncompetitive inhibition).

75
Q

Irreversible inhibitor forms a

A

a covalent bond within the active site that permanently prevents catalytic activity.

76
Q

Differentiate between enzymes and inhibitors.

A

Enzymes are the biological catalysts for reactions in our body. Catalyst is a substance which increases the speed of a chemical reaction by choosing another path for the reaction.
Inhibitors decrease enzyme activity by binding in active site (competitive inhibition) or at another site on the enzyme (noncompetitive inhibition). Irreversible inhibitor forms a covalent bond within the active site that permanently prevents catalytic activity.

77
Q

Proteins are

A

amino acid chains that fold into unique 3-dimensional structures.

78
Q

The shape into which a protein naturally folds is known as its

A

native state, which is determined by its sequence of amino acids and interaction of groups.

79
Q

The overall charge is zero for the neutral amino acid and is called a

A

zwitter ion

80
Q

are considered as the building blocks of proteins.

A

amino acids

81
Q

determines the properties of each amino acid because all 3 other groups attached to the alpha C atom are common for all amino acids.

A

the R group

82
Q

Due to the presence of a positive amino group and negative carboxyl group, amino acids have properties similar to a

A

salt

83
Q

groups H, alkyl and aryl are

A

non polar

hydrophobic

84
Q

groups OH, SH, CONH2

A

polar neutral

hydrophilic

85
Q

groups COOH

A

Polar acidic

hydrophilic

86
Q

Groups NH2

A

polar basic

hydrophilic

87
Q

The amide bond formed when amino acids combine through condensation reaction is known as a

A

peptide bond

88
Q

When 2 amino acids combine what forms

A

dipeptide

89
Q

Proteins are known as polymers due to the presence of

A

longer chains

90
Q

The repeating sequence of an amino acid is the

A

backbone of the dipeptide

91
Q

The process of breaking larger food molecules down into subunits small enough to diffuse through a cell membrane and to be used by the cell is termed

A

digestion

92
Q

catalyzes the digestion of carbs

A

amylase

93
Q

catalyzes digestion of proteins

A

pepsin

94
Q

helps in emulsifying fats in small intestine.

A

lipase

95
Q

These proteins are secreted by endocrine cells to control or regulate biological processes like growth, metabolism, and reproduction.

A

Hormones

96
Q

helps in regulating blood glucose levels.

A

insulin

97
Q

transports oxygen for use in cellular metabolism

A

hemoglobin

98
Q

act as an electron carrier in the electron transport chain.

A

Cytochromes

99
Q

in hair, nails and skin helps give these structures strength

A

keratin

100
Q

which is a structural protein found in various connective tissues, provides the framework for the ligaments that hold bones together and the tendons that attach muscles to those bones.

A

collagen

101
Q

recognize and destroy foreign pathogens in the immune system.

A

immunoglobulins

102
Q

helps in muscle contraction and movement. Contractile proteins can cause heart complications if they produce severe contractions.

A

Actin and Myosin

103
Q

Storage proteins mainly store

A

mineral ions such as potassium in your body.

104
Q

is required for the formation of hemoglobin, the main structural component of red blood cells

A

Iron

105
Q

a storage protein, regulates and guards against the adverse effects of excess iron in human body.

A

Ferritin

106
Q

Ovalbumin and casein are

A

are storage proteins found in breast milk and egg whites, respectively, that play a huge role in embryonic development

107
Q

naturally produced opiates in the body, are found in thalamus and spinal cord tissue. They are polypeptides that have pain-killing properties

A

Enkephalins

108
Q

actin and myosin

A

contractile

109
Q

lactase and pepsin

A

enzyme

110
Q

insulin, oxytocin, somatotropin

A

hormone

111
Q

keratin, collagen

A

structure

112
Q

ferritin

A

storage

113
Q

hemoglobin, cytochromes

A

transport

114
Q

elastin, dystrophin

A

support

115
Q

immunoglobulin

A

antibody

Chem 2 (9 decks)

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