Biochem Exam 2 Flashcards

1
Q

A peptide built from three amino acids must have

A

three side chains

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2
Q

What happens soonest during the protein folding process?

A

Hydrophobic groups move to the protein interior

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3
Q

At a pH above its pKa, the e-amino group of lysine is

A

deprotonated and neutral

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4
Q

What is the N-terminal residue of the peptide AYSDG?

A

Alanine

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5
Q

In an alpha helix, each carbonyl group

A

is a hydrogen bond acceptor

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6
Q

Which of the following amino acids is generally absent from an alpha-helix?

A

Proline

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7
Q

Which of the following is most critical for maintaining the tertiary structure of a protein?

A

hydrophobic interactions

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8
Q

Three of the 20 amino acids that are incorporated into proteins are aromatic. They are:

A

tyrosine, phenylalanine, and tryptophan

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9
Q

The predominant non-covalent interaction seen in alpha-helices and beta-sheets is

A

hydrogen bonds

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10
Q

Which statement is FALSE about the classification of amino acids?

A

Glutamic acid and asparagine are negatively charged amino acids

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11
Q

Which of the following best describes the side chains of the nonpolar amino acids (glycine is not included)?

A

They are primarily neutral hydrocarbon structures

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12
Q

If an alpha-helical region of a protein contained 18 amino acid residues, how many helical turns would be present?

A

5

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13
Q

Which of the following forces stabilize protein primary structure at physiological pH?

A

covalent bonds

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14
Q

Which of the following statements about peptide bonds in FALSE. Peptide bonds are:

A

charged

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15
Q

Amino acid residues with nonpolar side chains are mostly located in the protein interior because

A

nonpolar groups cannot interact with water molecules

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16
Q

Which of the following statements about the peptide bond is FALSE?

A

It is a phosphodiester bond

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17
Q

Which of the following is FALSE with respect to beta-sheets?

A

Amino acid side chains protrude from one side of the beta-sheet

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18
Q

Which of the following statements about the alpha-helix and beta-sheet are TRUE?
1. They are both types of secondary structure.
2. They are both stabilized by hydrogen bonds between amino acid side chains.
3. The polypeptide backbone is fully extended in both structures.
4. They are both usually located in the interior of soluble globular proteins

A

1 and 4

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19
Q

A domain is:

A

a folded segment of polypeptide with a separate hydrophobic core

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20
Q

What is the primary driving force in the formation of protein tertiary structure?

A

The exclusion of non-polar substances from aqueous solution

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21
Q

What ultimately determines the unique three-dimensional structure of soluble globular proteins?

A

The sequence of the amino acid residues

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22
Q

A polypeptide that does not assume its proper three-dimensional structure

A

may be degraded, may re-fold, may accumulate

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23
Q

To dislodge a protein bound to a carboxymethyl column, you should add a solution containing

A

a higher concentration of cations

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24
Q

Hemoglobin’s oxygen-binding curve is sigmoidal because

A

O2 binding shifts hemoglobin to a high-affinity conformation

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25
Respiring tissues release CO2, which leads to
a shift to the T state of hemoglobin
26
Calculate the fractional saturation for myoglobin when pO2 is a. 20 torr and b. 80 torr.
The fractional saturation at 20 and 80 torrs are 0.88 and 0.97, respectively, which indicate the myoglobin is 88% and 97% saturated with oxygen at these respective pressures
27
A protein that consists of more than one polypeptide chain has
quaternary structure
28
Which of the following statements is FALSE? In its interaction with hemoglobin, oxygen is:
a prosthetic group
29
Structurally, myoglobin and hemoglobin are very similar proteins. In which of the following levels of structure do they differ most?
Quaternary structure
30
Which cytoskeletal proteins are constructed from globular protein subunits?
actin filaments and microtubules
31
The changes in cell shape that allow crawling are mainly the result of
actin filament assembly and disassembly
32
Which type of structural protein is exclusively extracellular?
collagen
33
Phalloidin, a peptide isolated from a poisonous mushroom, binds to F-actin but not G-actin. How does the addition of phalloidin affect cell motility?
cell mobility is impared
34
The motor protein myosin has
two heads attached to a rigid neck lever
35
Straight hair can be curled and curly hair can be straightened by exposing wet hair to a reducing agent, repositioning the hair with rollers, then exposing the hair to an oxidizing agent. What are the roles of the reducing and oxidizing agents?
The reducing agent breaks disulfide bonds; the oxidizing agent forms new disulfide bonds
36
"Hard" keratins such as those found in hair, horn, and nails have a high sulfur content whereas "soft" keratins found in the skin have a lower sulfur content. Explain the structural basis for this observation.
Hard keratins have oxidized cysteine residues, which enhance stability through disulfide bonds
37
Kinesin is known as a processive motor because
it remains attached to its track after each reaction cycle
38
Which of the following amino acids has the most significant role in the molecular mechanisms of hemoglobin's function?
histidine
39
Is myosin a fibrous protein or a globular protein?
it's both fibrous and globular
40
Which of the following best describes the tertiary structure of myoglobin?
it contains heme, which is slotted into a hydrophobic pocket between alpha-helix E and alpha-helix F
41
Which of the following statements about 2,3-bisphosphoglycerate (BPG) binding is FALSE?
BPG aids oxygen delivery to tissues by increasing the affinity of myoglobin for oxygen
42
Which of the following statements about the structure of myoglobin is FALSE?
Myoglobin contains all three types of secondary structure
43
A newly-identified protein has a sigmoidal curve in a graph of fractional saturation versus ligand concentration. What can be deduced about this protein?
The protein binds the ligand cooperatively
44
Myoglobin and hemoglobin are both oxygen-binding proteins but have very different physiological roles. Which two of the following are the most important factors that contribute to their different functions?
Myoglobin is a monomeric protein, whereas hemoglobin is a tetrameric protien Hemoglobin binds BPG which stabilizes the deoxy (T) state
45
Which of the following statements most accurately explains why hemoglobin is able to deliver oxygen to myoglobin in the tissues?
Myoglobin has a hyperbolic oxygen binding curve, whereas hemoglobin has a sigmoidal oxygen binding curve
46
Why is BPG essential for the delivery of O2 to the tissues?
BPG stabilizes the T state conformation of hemoglobin
47
Which of the following is a role of histidine in myoglobin?
A histidine residue forms a hydrogen bond with oxygen
48
The binding of one O2 to a molecule of hemoglobin results in:
An increased affinity for O2 in the remaining subunits (Which have not yet bound O2)
49
Which of the following statements about the structure of myoglobin is TRUE?
A heme prosthetic group is tightly bound to myoglobin via coordination bond
50
What is the fractional saturation of myoglobin at pO2 = 7.2 torr, if P50 = 2.8 torr?
0.72
51
Proteins such as hemoglobin are known as ______ proteins since binding of a molecule to one site alter binding to other sites
allosteric
52
During the formation of microfilaments, which of the following occurs?
ATP hydrolysis is catalyzed by F-actin
53
The idea that binding of one molecule of oxygen to hemoglobin enhances further binding of oxygen to hemoglobin is called
cooperativity
54
Proteins such as hemoglobin are known as _______ proteins since binding of a molecule of one site alter binding to other sites
allosteric
55
When oxygen is bound to the heme group of myoglobin, it is coordinated between
E7 His; Fe2+ of heme
56
Which allosteric effector has the greatest ability to stabilize the deoxy state of hemoglobin?
BPG
57
What is the prominent type of secondary structure observed in myoglobin?
alpha-helices
58
The individual hemoglobin subunits and myoglobin share what similar structures but have what different structures
secondary and tertiary; primary
59
Which amino acid is critical for crosslinking of collagen trimers?
Lys
60
In a muscle cell, what is the name for the bundles of myosin tails?
thick filaments
61
Which of the following fibers is correctly paired with the protein that forms fibers
microfilaments: actin microtubule: tubulin extracellular support fibers: collagen intermediate filaments: keratin
62
Which of the following details the nucleotide-binding side when tubulin dimers assemble into microtubules?
the alpha site is bound to GTP; the beta site is bound to GDP
63
Which of the following details the nucleotide-binding site when tubulin dimers assemble into microtubules
the alpha site is bout to GTP; the beta site is bound to GDP
64
When a cell moves along a surface' actin _____ occurs at the leading edge while _______ occurs at the trailing edge
polymerization; depolymerization
65
While the composition of hemoglobin in adult humans is alpha2 beta 2, in the developing fetus, ______ is observed
alpha2 y2
66
In a solution of high pH (<12), all of the acidic and basic sites in an amino acid are
deprotonated
67
Parallel polypeptide chains in a beta-pleated sheet conformation are held together by
hydrogen bonding
68
Which of the following would be a correct representation of a portion of a protein "backbone"?
the one with two peptide bonds on either side of an amino acid
69
Which of the following best describes the peptide backbones in a beta-sheet?
highly extended
70
Glycine, the simplest amino acid, is different from all of the other standard amino acids in that it
does not have a chiral center
71
The first step in the folding of disordered polypeptide chains into stable proteins is the formation of:
secondary structural elements
72
Which one of these characteristics is not true for the alpha helix?
there is a requirement for glycine every third amino acid residue
73
Which of the following amino acids is most likely to be found on the interior of a protein (Use the Hydrophobic Scale from your textbook)
methionine
74
Molecular chaperones assist proteins in the formation of
tertiary structure
75
Which of the following amino acids would be classified as a polar neutral amino acid?
The amino acid that has a neutral charge
76
What enzyme is required to form a new phosphodiester bond when inserting DNA into a plasmid?
ligase
77
Which bond is unable to rotate?
peptide bond
78
Which of the following has the most dramatic influence on the characteristics of an individual natural protein:
the amino acid sequence
79
Which of the following is a palindromic sequence?
GAATTC
80
Which of the following statements concerning the tripeptide Val-Ala-Gly is correct?
The C-terminal amino acid residue is Gly