CELLULAR AND MOLECULAR
BIOLOGY FINAL EXAM NEWEST
ACTUAL EXAM 2024-2025 QUESTIONS
AND DETAILED CORRECT ANSWERS |
VERIFIED ANSWERS
The three dimensional details of a specimen can be
collected when using:
-(A) The light microscope,
-(B) The transmission electron microscope,
-(C) Image deconvolution,
-(D) Formaldehyde fixatives. Correct Answer (C)
Which of the following is the best microscope to use in
order to collect two dimensional details of a specimen's
interior at very high magnification:
-(A) The light microscope,
-(B) The confocal microscope,
-(C) The transmission electron microscope,
-(D) The scanning electron microscope. Correct Answer
(C)
Specific three dimensional details in a biological
specimen's interior can most effectively be evaluated
when using:
-(A) Brightfield microscopy,
-(B) The transmission electron microscope,
,-(C) The confocal microscope,
-(D) The scanning electron microscope. Correct Answer
(C)
A protein that traversed the nuclear membrane of the cell
in an alpha helix would tend to have the following
characteristics within the transmembrane segment:
-(A) polar side groups
-(B) a hydrophobic backbone
-(C) non-polar side groups
-(D) covalent attachment to surrounding lipid molecules
-(E) none of the above Correct Answer (C)
A protein composed almost entirely from beta sheets
would have the following characteristics:
-(A) mostly polar side groups
-(B) mostly nonpolar side groups
-(C) The individual strands of the sheet held together by
ionic bonds between peptide bonds in different strands
-(D) A very rigid structure
-(E) none of the above Correct Answer (E)
What type of interaction will these two amino acid side
chains experience?
-(A) hydrogen bonds
-(B) electrostatic interactions
-(C) Van der Waals
-(D) hydrophobic force Correct Answer (B)
In general, ionic bonds within a folded protein structure
can form between atoms of two peptide bonds, between
,atoms of a peptide bond and an amino acid side chain,
and between two amino acid side chains.
-(A) True
-(B) False Correct Answer (B)
Why is the particular three-dimensional folded
conformation of a protein so important?
-(A) it dictates whether the protein will be mobile in the
cytoplasm, anchored to a plasma membrane, or serve a
structural role,
-(B) it dictates whether or not two different or identical
proteins will interact,
-(C) it dictates the mechanical strength of the protein,
-(D) all of the above,
-(E) none of the above. Correct Answer (D)
The alpha helix or beta sheet present within a protein
makes the entire protein very rigid.
-(A) True
-(B) False Correct Answer (B)
What type of interaction will these two amino acids
experience?
-(A) hydrogen bonds
-(B) electrostatic interactions
-(C) Van der Waals
-(D) hydrophobic force Correct Answer (A)
What properties will these amino acids confer to the
peptide chain?
-(A) Glycine-hydrophilicity; Proline-hydrophobicity
Protein domain is the term used to describe structurally
stable independent regions within one polypeptide chain,
which are usually connected to each other by relatively
short and unstructured polypeptide segments.
-(A) True
-(B) False Correct Answer (A)
Spontaneous protein folding implies that all the information
needed for specifying the three-dimensional shape of a
protein is contained in its amino acid sequence, which is
derived from the unique sequence of DNA that encodes
each protein.
-(A) True
-(B) False Correct Answer (A)
In signaling through G proteins and GPCRs, which one of
the following is true:
-(A) the GDP is part of the chemical structure of the G
protein
-(B) the extracellular signal moleculeactivates the G
protein by binding directly to the G protein
-(C) The GPCR is made up primarily of rigid alpha helices
and therefore does not change its shape
-(D) all of the above
-(E) none of the above Correct Answer (E)
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