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BCH 210 Exam 2 Multiple Choice|40 Complete Questions and Answers|2023
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BCH 210 Exam 2 Multiple Choice|40Complete Questions and Answers|2023
1. When a protein is ingested & encounters the acidity of the stomach (pH
1.0), its tertiary structure will be disrupted. A non covalent interaction that
will be broken will be salt bridges within the protein because the _______
group (pKa 3.5) will become protonated. This will result in an excess of ______
charges on the protein and the electro-repulsion will further disrupt
structure.
A) Amino; Negative
B) Amino; Positive
C) Carboxyl; Negative
D) Carboxyl; Positive - -D) Carboxyl; Positive
-2. A small peptide leaving the stomach for the small intestine has an amino
acid sequence of: H3N+-Arg-Pro-Pro-Gly-Tyr-Ser-Pro-Phe-Arg-COO^- in the
small intestine this peptide is further hydrolyzed to give the following
products
i. H3N+-Arg-Pro-Pro-Gly-Tyr-COO^-
ii. H3N+-Ser-Pro-Phe-COO^-
iii. H3N+-Arg-COO^-
What enzyme was responsible for these cleavages?
A) Pepsin
B) Trypsin
C) Chymotrypsin
D) Carbonic anhydrase - -C) Chymotrypsin
-3. The enzyme, trypsin, is a protease that hydrolyzes oligopeptides in the
small intestine. One of the remarkable things is that, in its journey from the
pancreas to the small intestine, trypsin does not act as a wrecking ball
destroying the walls of the pancreatic duct by hydrolyzing proteins, why
would this be?
A) Trypsin is synthesized in an inactive precursor form, a zygomen, and not
activated until it reaches the small intestine.
B) Trypsin is enveloped by Chaperonin as it moves to the small intestine;
thus preventing its proteolytic action until the Chaperonin dissociates in the
intestine.
C) The pH of the pancreatic duct does not permit trypsin activity while in
transit to the small intestine - -A) Trypsin is synthesized in an inactive
precursor form, a zygomen, and not activated until it reaches the small
intestine.
, -4. Repeating structural non covalent bonds, which make up secondary
structures of polypeptides (such as alpha-helices and beta pleated sheets),
are predominantly formed as a result of:
A) Hydrogen bonding from the peptide side chains ("R" groups)
B) Hydrogen bonding from the peptide backbone
C) Hydrophobic interactions
D) All of the above - -B) Hydrogen bonding from the peptide backbone
-5. Which property does NOT belong with the others in describing an alpha-
helix?
A) Peptide backbone is fully extended
B) H bonds are parallel
C) All "R" groups lie outside of the helix
D) H bonds are intrastrand - -A) Peptide backbone is fully extended
-6. Which of the following amino acids would act to destroy an alpha-helix?
A) Glycine
B) Serine
C) Proline
D) All of the above - -D) All of the above
-7. A sequence of amino acids in a certain protein is found to be -Ser-Gly-
Pro-Gly. The sequence is most likely part of a(n):
A) Antiparallel beta sheet
B) Alpha helix
C) Beta reverse turn
D) B-strand - -C) Beta reverse turn
-8. Which property of the Beta pleated sheet of secondary structure does
NOT belong?
A) Hydrogen bonds are perpendicular to the direction of the B-strands
B) The polypeptide B strands are almost fully extended
C) The polypeptide B strands are frequently hydrogen bonded together in an
antiparallel orientation
D) Hydrogen bonds are intrastrand
E) R groups alternate above and below the plane of the B-sheet - -D)
Hydrogen bonds are intrastrand
-9. A feature of super secondary structure in globular protein is the "motif".
A commonly used motif by Mother Nature is the B-meander. When this
structural unit is repeated, it can form a "B-barrel", a larger unit of super
secondary structure called a _________. Proteins such as immunoglobulin
have a number of these regions.
A) Module
B) Oligomer
C) Site
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