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CHEM 101 > FT LEC: Proteins and Enzymes > Flashcards

FT LEC: Proteins and Enzymes Flashcards

1
Q

All _________ contain the elements carbon, hydrogen, oxygen, and nitrogen; most also contain sulfur

A

PROTEINS

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2
Q

the main protein of milk, contains phosphorus

A

Casein

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2
Q

Other elements, such as phosphorus and iron, are essential constituents of certain specialized proteins

A
  1. Casein
  2. Hemoglobin
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2
Q

The presence of nitrogen sets them apart from carbohydrates and lipids, which most often do not contain nitrogen.

A

PROTEINS

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3
Q

the oxygen-transporting protein of blood, contains iron

A

Hemoglobin

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4
Q

Casein, the main protein of milk, contains ________

A

phosphorus

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5
Q

Hemoglobin, the oxygen-transporting protein of blood, contains _______

A

iron

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6
Q

Proteins are naturally occurring polymers in which the monomer units are ________

A

amino acids

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7
Q

The Building Blocks for Proteins

A

AMINO ACIDS

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8
Q

an organic compound that contains both an amino (-NH2) group and a carboxyl (-COOH) group

A

AMINO ACIDS

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9
Q

Amino acids found in proteins

A

α-amino acid

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10
Q

the amino group and the carboxyl group are attached to the α-carbon atom

A

α-amino acid

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11
Q

distinguishes α-amino acids from each other

A

R group

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12
Q

amino acid side chain

A

R group

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13
Q

STANDARD AMINO ACIDS

A
  1. Nonpolar Amino Acid
  2. Polar Amino Acid
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14
Q

has nonpolar side chain

A

Nonpolar Amino Acid

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15
Q

hydrophobic (water-fearing)

A

Nonpolar Amino Acid

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16
Q

Found in the interior of proteins, where there is limited contact with water

A

Nonpolar Amino Acid

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17
Q

R group – hydrocarbons (aliphatic or aromatic)

A

Nonpolar Amino Acid

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18
Q

has polar side chain

A

Polar Amino Acid

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19
Q

hydrophilic (water-loving)

A

Polar Amino Acid

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20
Q

Found on the surfaces of proteins

A

Polar Amino Acid

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21
Q

Subcategorized to: Polar neutral, polar acidic, and polar basic

A

Polar Amino Acid

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22
Q

Side chain of Polar neutral

A

has groups containing heteroatoms

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22
Q

TYPES OF POLAR AMINO ACIDS

A
  1. Polar Neutral
  2. Polar Acidic
  3. Polar Basic
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23
Q

contain polar but neutral side chain (R group)

A

Polar neutral

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24
Q

contain a carboxyl group as part of the side chains

A

Polar acidic

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25
Q

Side chain of polar acidic:

A

carboxylic acid

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26
Q

contain an amino group as part of the side chain

A

Polar basic

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27
Q

Side chain of polar basic

A

amine, imine

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28
Q

The ________ of one amino acid interacts with the amino group of the other amino acid.

A

carboxyl group

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29
Q

Amino acids are linked together by an _______

A

amide (peptide) bond via a condensation reaction

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30
Q

The four levels of protein structure are

A

Primary (1o)
Secondary (2o)
Tertiary (3o)
Quaternary (4o)

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31
Q

Amino acid sequence

A

Primary (1o)

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32
Q

Overall 3D shape of folded protein

A

Tertiary (3o)

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32
Q

H-bonds on protein backbone

A

Secondary (2o)

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33
Q

Subunit organization

A

Quaternary (4o)

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34
Q

is the order/sequence in which amino acids are linked together in a protein

A

PRIMARY STUCTURE (1o)

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35
Q

Amino acids are linked to each other by ____________

A

peptide bonds

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36
Q

Arrangement in space adopted by the hydrogen-bonded arrangement of the backbone portion of a protein

A

SECONDARY STRUCTURE (2o)

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37
Q

Common types of secondary structures

A
  1. α helix
  2. β pleated sheet (β-sheet)
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37
Q

Folding is stabilized by noncovalent interactions

A

SECONDARY STRUCTURE (2o)

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38
Q

Composed of 1 polypeptide chain

A

α helix

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39
Q

H bonds are within a single polypeptide chain (backbone only)

A

α helix

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40
Q

R-groups are outside

A

α helix

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41
Q

Right-handed or clockwise, spiral

A

α helix

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42
Q

Composed of two or more polypeptide chains

A

β pleated sheet (β-sheet)

43
Q

H-bonds are between adjacent strands

A

β pleated sheet (β-sheet)

44
Q

H-bonds are between adjacent strands

A

β pleated sheet (β-sheet)

45
Q

A single protein chain adopts a shape that resembles a coiled spring (helix)

A

ALPHA-HELIX STRUCTURE

46
Q

Coil configuration maintained by

A

hydrogen bonds

47
Q

Two fully extended protein chain segments in the same or different molecules

A

BETA-PLEATED SHEET STRUCTURE

47
Q

Twist of the helix forms a

A

right-handed, or clockwise, spiral

48
Q

Hydrogen bonds between C=O and N—H entities are orientated ________ to the axis of the helix

A

parallel

49
Q

Overall three-dimensional shape of a protein

A

TERTIARY STRUCTURE (3o)

50
Q

chains (R groups) that are widely separated from each other

A

TERTIARY STRUCTURE (3o)

51
Q

There are two main factors for folding of a protein:

A
  • hydrophobic residues
  • polar residues
52
Q

Covalent, strong, and involve two cysteine units

A

Covalent disulfide bonds

53
Q

Can occur between amino acids with polar R groups

A

Hydrogen bonds

53
Q

Involve the interaction between charged side chains of acidic and basic amino acids

A

Electrostatic attractions (salt bridges)

54
Q

Occur when two nonpolar side chains are close to each other

A

Hydrophobic attractions

55
Q

Highest level of protein organization

A

QUATERNARY STRUCTURE (4o)

55
Q

Organization among the various peptide subunits in a multimeric protein

A

QUATERNARY STRUCTURE (4o)

56
Q

found in proteins that have two or more polypeptide chains (subunits)

A

QUATERNARY STRUCTURE (4o)

57
Q

Subunits are independent of each other and not covalently bonded to each other

A

QUATERNARY STRUCTURE (4o)

58
Q

Contain even number of subunits

A

QUATERNARY STRUCTURE (4o)

59
Q

Reverse of peptide bond formation

A

PROTEIN HYDROLYSIS

60
Q

Results in the regeneration of an amine and carboxylic acid functional groups

A

PROTEIN HYDROLYSIS

61
Q

is when all peptide bonds are broken, and the only products are amino acids

A

Complete hydrolysis

62
Q

is when some but not all peptide bonds are broken, and the product is a mixture of amino acids and small peptides

A

Partial hydrolysis

63
Q

Partial or complete disorganization of a protein’s characteristic three-dimensional shape

A

PROTEIN DENATURATION

64
Q

Filamentous or elongated shape

A

FIBROUS PROTEIN

64
Q

PROTEIN CLASSIFICATION BASED ON SHAPE

A
  1. FIBROUS PROTEIN
  2. GLOBULAR PROTEIN
65
Q

Function is mostly structural (strength/support)

A

FIBROUS PROTEIN

66
Q

Repetitive AA sequence

A

FIBROUS PROTEIN

67
Q

Usually water-insoluble

A

FIBROUS PROTEIN

68
Q

Provide protective coating for organisms

A

α-Keratin

69
Q

Major protein constituent of hair, feather, nails, horns, and turtle shells

A

α-Keratin

70
Q

Mainly made of hydrophobic amino acid residues

A

α-Keratin

71
Q

Most abundant protein in humans

A

COLLAGEN

72
Q

Organic component of bones and teeth

A

COLLAGEN

73
Q

Major structural material in tendons, ligaments, blood vessels, and skin

A

COLLAGEN

74
Q

help maintain the structure of the triple-helix

A

Glycine and proline

75
Q

Spherical or globular shape

A

GLOBULAR PROTEIN

76
Q

Function is mostly as catalyst, transport, etc.

A

GLOBULAR PROTEIN

77
Q

irregular AA sequence

A

GLOBULAR PROTEIN

78
Q

Usually, water-soluble

A

GLOBULAR PROTEIN

79
Q

Oxygen-storage molecule in muscles

A

MYOGLOBIN

80
Q

Consists of a single peptide chain and one heme unit

A

Monomer

81
Q

An oxygen-carrier molecule in blood

A

HEMOGLOBIN

82
Q

Each subunit contains a heme group (four polypeptide chains)

A

Tetramer

83
Q

A compound, usually a PROTEIN, that acts as a CATALYST for a biochemical reaction.

A

ENZYME

84
Q

Most enzymes are __________

A

GLOBULAR PROTEINS

85
Q

enzyme composed only of protein (amino acid chains)

A

Simple enzyme

86
Q

enzyme that has a nonprotein and protein parts

A

Conjugated enzyme

87
Q

Redox reactions

A

Oxidoreductase

88
Q

CLASSES OF ENZYME

A

Ligase
Isomerase
Lyase
Hydrolase
Oxidoreductase
Transferase

89
Q

Transfer of functional groups

A

Transferase

90
Q

Isomerization

A

Isomerase

90
Q

Hydrolysis reactions

A

Hydrolase

90
Q

Addition of groups to double bonds or removal of groups to form double bonds

A

Lyase

91
Q

Joining of two molecules (hydrolysis of ATP as energy source)

A

Ligase

92
Q

an enzyme that catalyzes an oxidation-reduction reaction

A

OXIDOREDUCTASE

93
Q

an enzyme that catalyzes the transfer of a functional group from one molecule to another

A

TRANSFERASE

94
Q

help disposal of nitrogen during the metabolism of amino acids for energy production or for synthesis of bioactive compounds from amino acids

A

Aminotransferases

95
Q

an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break

A

HYDROLASE

96
Q

effect the breaking of glycosidic bonds in oligo- and polysaccharides

A

Carbohydrases

97
Q

effect the breaking of peptide linkages in proteins

A

Proteases

98
Q

effect the breaking of ester linkages in triacylglycerols

A

Lipases

99
Q

an enzyme that catalyzes addition or removal of atoms across a double bond

A

LYASE

100
Q

adds water across the double bond in trans-Enoyl CoA during the oxidation of fatty acids for biochemical energy production

A

Enoyl CoA hydratase

101
Q

small part of an enzyme’s structure that is involved in catalysis; it is where the substrate binds to the enzyme

A

ACTIVE SITE

102
Q

formed due to folding and bending of the protein

A

ACTIVE SITE

103
Q

“CREVICE-LIKE” location in the enzyme

A

ACTIVE SITE

104
Q

contains catalytic amino acid residues or groups

A

ACTIVE SITE

105
Q

FACTORS AFFECTING ENZYME ACTIVITY

A
  • Temperature
  • pH
  • Substrate Concentration
  • Enzyme Concentration
105
Q

is the maximum amount of substrate molecules that an enzyme can convert to products

A

Turnover number

CHEM 101 (12 decks)

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