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biochem > W. 5 ch 16 amino acids > Flashcards

W. 5 ch 16 amino acids Flashcards

(81 cards)

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1
Q

Which of the following is not a function of proteins?

A

stores the genetic information of a living organism

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2
Q

Collagen, a protein found in tendons and cartilage, would be classified as a _____ protein.

A

structural

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3
Q

Sucrase, the protein that facilitates the hydrolysis of sucrose, would be classified as a _____ protein.

A

catalytic

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4
Q

A basic amino acid has a side chain that contains ______.

A

an ammonium group

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5
Q

In the ionized form of an amino acid, the carboxylic acid end is _____.

A

negatively charged

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6
Q

Methionine is an amino acid that contains _____.

A

a sulfur atom

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7
Q

The structural formulas of amino acids are the same except for the _____.

A

R group

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8
Q

Wool is primarily made up of _____.

A

protein

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9
Q

The following amino acid side chain is ______.

A

hydrophobic

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10
Q

The R group for serine is -CH₂-OH. In the ionized form, serine has the structural formula _____.

A
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11
Q

Which of the following functional groups of an amino acid would be in the ionized state at high pH?

A
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12
Q

The side chain for histidine is classified as a _____ side chain.

A

basic

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13
Q

The side chain for valine is classified as a ____ side chain.

A

nonpolar

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14
Q

Which of the following would be most likely to be deficient in at least one essential amino acid?

A

beans

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15
Q

Amino acids that are not synthesized in the body and must be obtained from the diet are called ______.

A

essential

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16
Q

A completely vegetarian diet will contain all the essential amino acids if it includes _____.

A

rice and beans

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17
Q

The one-letter abbreviation for the amino acid tryptophan is _____.

A

W

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18
Q

The one-letter abbreviation for the amino acid tyrosine is _____.

A

Y

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19
Q

The peptide bonds that link amino acids in a protein are _____.

A

amide bonds

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20
Q

In the peptide STFNA, the N-terminus is _____.

A

serine

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21
Q

In the peptide Ala-Try-Gly-Phe, the N-terminus is _____.

A

alanine

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22
Q

In the peptide Ser-Cys-Ala-Gly, the C-terminus is _____.

A

glycine

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23
Q

In the peptide GLVIW, the C-terminus is ____.

A

tryptophan

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24
Q

A chain made of more than 50 amino acids that has biological activity is referred to as a _____.

A

protein

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25
Enkephalins are polypeptides that have _____.
pain-killing properties
26
In insulin, two peptide chains are held together in a single unit by _____.
disulfide bridges
27
The attractive forces that are important in the secondary structure of a protein are _____.
hydrogen bonds
28
Which of the following is a secondary protein structure?
a-helix
29
Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein?
30
What type of interaction would you expect between the following R groups in the tertiary structure of a protein?
salt bridges
31
What type of interaction would you expect between the following R groups in the tertiary structure of a protein?
hydrophobic interaction
32
What kinds of interactions are not part of tertiary protein structure?
peptide bonds
33
Acids and bases denature a protein by disrupting _____.
salt bridges and hydrogen bonds
34
Heat denatures a protein by disrupting ____.
hydrophobic interactions and hydrogen bonds
35
The structure of collagen consists of ____.
a braided triple helix
36
The α helix of the secondary structure of a protein is held together by ____ between two widely separated parts of a protein chain.
hydrogen bonds
37
In the β-pleated sheet secondary structure of a protein, two or more amino acid sequences in separate parts of the protein are held together ____.
by hydrogen bonding between different sections of the polypeptide chain
38
Hemoglobin has a total of _____ protein chains in its quaternary structure.
four
39
In the sickle-cell anemia, the hemoglobin molecules _____.
clump together into insoluble figures
40
Denaturation of a protein ____.
disrupts the secondary, tertiary, or quaternary structure of a protein.
41
One heavy metal that can cause denaturation of a protein is ____.
silver
42
Heavy metals denature proteins by ____.
disrupting disulfide bonds
43
An acid can denature a protein by _____.
disrupting hydrogen bonds between side chains
44
Disulfide bonds in a protein chain connect ____.
two cysteine residues
45
To what main class of enzyme does the enzyme that catalyzes the conversion of lactose to galactose and glucose belong?
hydrolase
46
The purpose of many chemical reactions in our bodies is to _____.
store chemical energy in the body for future use, produce the amino acids, produce the lipids, and release chemical energy for the production of macromolecules.
47
To what main class of enzymes does the enzyme that catalyzes the following reaction belong?
oxidoreductase
48
To what main class of enzymes does the enzyme that catalyzes the following reaction belong? ser—ala → ser + ala
hydrolase
49
Compared to an uncatalyzed reaction, an enzyme-catalyzed reaction ______.
occurs at a faster rate
50
The general function of an enzyme in the body is to _____.
catalyze chemical reactions
51
A biological catalyst is called a _____.
enzyme
52
The full name of the enzyme LDH is _____.
lactate dehydrogenase
53
The names of many enzymes can be recognized by the suffix ____.
ase
54
The hydrolysis of ester bonds in triacylglycerols is catalyzed by a _____.
lipase
55
Most enzymes are _____.
globular proteins
56
The presence of enzymes to catalyze bioreactions in our bodies allows ____.
bioreactions to take place under mild conditions
57
The formation of an enzyme-substrate complex is the _____ step in enzyme action.
first
58
The active site of an enzyme _____.
is the region where the reaction takes place
59
The optimum temperature for sucrase activity is 37°C. The hydrolysis of sucrose is slowest at which temperature in the choices below?
0 °C
60
Which of the following is not true for a competitive inhibitor?
it binds to the enzyme at a site remote from the active site
61
A noncompetitive inhibitor _____.
alters the three-dimensional structure of the enzyme
62
"Physiological conditions" for reactions within the body are approximately _____.
pH 7.4 and 37 °C
63
"Physiological pH," the pH for optimum activity for most enzymes, is a pH equal to about _____.
7.4
64
In the lock-and-key model of enzyme action, the enzyme active site is thought of as ______.
a rigid, nonflexible shape that fits the substrate exactly
65
In the induced-fit model of enzyme action, the enzyme active site _____.
adjusts shape to adapt to the shape of the substrate
66
The function of the enzyme-substrate complex is to provide an alternative reaction pathway that ____.
lowers the activation energy for the reaction
67
Most enzymes are deactivated permanently above a temperature of about _____.
50 °C
68
Urea is converted to ammonia and carbon dioxide by the action of urease. What will be the effect on the rate if the temperature of the reaction is lowered from 37 °C (the optimum temperature) to 27 °C?
The rate will slow down
69
A competitive inhibitor is one that ____.
binds to the active site in place of the substrate
70
A noncompetitive inhibitor has a structure that _____.
does not resemble the substrate structure
71
A compound that binds to an enzyme and changes its shape so that a substrate cannot enter the active site is called a ______.
noncompetitive inhibitor
72
Enzymes that catalyze the same reactions but have slightly different structures are called _____.
isoenzymes
73
The optimum pH for the activity of pepsin is about ____.
2.0
74
Immunoglobulin, a protein that stimulates immune responses, would be classified as a ____ protein.
protection
75
What type of amino acids has polar side chains that are attracted to water?
hydrophilic
76
Consider the R groups of the following amino acids: cysteine: -CH₂SH; alanine: -CH₃; serine: -CH₂OH The name for the dipeptide shown below is _____.
alanylserine
77
In an enzyme, the polypeptide chain folds into a compact shape known as the _____ structure.
tertiary
78
When two protein chains combine to form an active protein, the structural level is _____.
quaternary
79
Hydrophobic interactions help to stabilize the _____ structure of a protein.
tertiary and quaternary
80
An enzyme that removes H atoms to form a double is a _____.
oxidoreductase
81
What process occurs when heat, acids, bases, and heavy metal ions cause a loss of biological function of a protein?
denaturation

biochem (8 decks)

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