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MOLECULAR BIOLOGY OF THE CELL 6TH EDITION BRUCE ALBERTS TEST BANK 2025 CHAPTER 3: PROTEINS
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MOLECULAR BIOLOGY OF THE CELL 6TH EDITION BRUCE ALBERTS TEST BANK 2025 CHAPTER 3: PROTEINS
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Samenvatting Molecular Biology of the Cell Deel Eén- Moleculair biology of the cell (BMW33416)
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MOLECULAR BIOLOGY OF THE CELL 6TH
EDITION BRUCE ALBERTS TESTBANK 2025
CHAPTER 3: PROTEINS
MOLECULAR BIOLOGY OF THE CELL, SIXTH EDITIONCHAPTER 3: PROTEINS
At physiological pH, what is the approximate net charge of a hexapeptide with the
following amino acid sequence?
Asp-Val-Ile-Glu-Arg-Ser
32
31
D. +1
E. +2
, lOMoAR cPSD| 37668344
Which of the following pairs of amino acid residues would you expect to form ionic
bonds?
Glutamic acid and glutamine
Arginine and lysine
Lysine and glutamic acid
Tryptophan and tyrosine
Tyrosine and glutamine
Which of the following stretches of amino acid residues would you expect to find in the
interior of protein molecules?
Ala-Asp-Asp-Tyr-Arg
Gly-Lys-Ser-Pro-Thr
Phe-Glu-Gln-Glu-Asn
Ala-Val-Leu-Ile-Trp
Gly-Tyr-His-Arg-His
Which of the following is NOT the role of molecular chaperones in the folding of cellular
proteins?
They assist proteins in folding into their correct conformations.
They help prevent formation of protein aggregates.
They specify the final three-dimensional shape of proteins.
They catalyze the folding of proteins in the crowded environment of the cell.
, lOMoAR cPSD| 37668344
They make the protein-folding process in the cell more reliable.
The observation that proteins often renature into their original conformations after they
have been unfolded by denaturing solvents implies that &
the information needed to specify the three-dimensional shape of a protein is encoded
in its amino acid sequence.
the cell does not need molecular chaperones for survival.
the final folded structure of a protein is usually NOT the one with the lowest free
energy.
each protein folds into several different conformations inside the cell.
All of the above.
Imagine a cellular protein composed of 3000 amino acid residues in one continuous
polypeptide chain. This protein is almost certainly &
extracellular.
globular.
multidomain.
composed of mostly a-helical regions.
intrinsically disordered.
For each of the following cartoon representations from left to right, indicate whether the
repetitive secondary structure elements. Your answer would be a four-digit number composed of
Images created in PyMOL, from PDB entries 1STU, 2LPC, 1SA8, and 3BOB.
Downloaded by mary daniel (mary011daniel@gmail.com)
, lOMoAR cPSD| 37668344
hydrogen-bonding between the amino acid side chains defines the type of secondary
structure.
a certain short amino acid sequence always adopts the same secondary structure.
only a few specific amino acid sequences can adopt these repetitive structures.
the folding patterns result from hydrogen-bonding between the N3H and C=O groups
in the polypeptide backbone.
All of the above.
Which of the following is NOT true regarding the members of a protein family in
general?
They have similar three-dimensional conformations.
They share an ancestry; i.e. they are homologs.
They can functionally replace each other.
Their gene sequence is less well conserved than their structure.
Over evolutionary time scales, the family has expanded mainly through gene
duplication events.
The number of ways in which protein domains fold in nature is limited. Which of the
following is a better estimate of this number?
A. 200
B. 2000
C. 200,000
D. 2,000,000
E. 20 million
The human estrogen receptor is a symmetrical dimeric nuclear protein that can regulate
gene expression by binding to a DNA sequence called an estrogen response element (ERE) near
the promoter of its target genes. Each subunit of the receptor binds to about six base pairs of
DNA. Which of the following sequences is a likely candidate for the ERE? The sequences are
AGGTCANNNTGACCT
AGGTCANNNAGGTCA
AGGTCANNNACTGGA
AGGTCANNNATATAT
Downloaded by mary daniel (mary011daniel@gmail.com)
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