BCHM 307 Quiz 2- All Questions100% Solved with Verified Solutions
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Course
BCHM 307
Institution
BCHM 307
What is most critical for maintaining the tertiary structure of a protein? - Answer
Hydrophobic interactions
What level of protein structure is characterized by the three dimensional structure of an
entire polypeptide including all amino acid side chains? - Answer Tertiary
What is the N-Termina...
BCHM 307 Quiz 2- All Questions100% Solved
with Verified Solutions
What is most critical for maintaining the tertiary structure of a protein? - Answer
Hydrophobic interactions
What level of protein structure is characterized by the three dimensional structure of an
entire polypeptide including all amino acid side chains? - Answer Tertiary
What is the N-Terminal residue of the peptide AYSDG - Answer Alanine
The amino acid _______ is commonly phosphorylated - Answer Ser
At a pH above its pKa, the epsilon-amino group of lysine is ____. - Answer Deprotonated
and neutral
Which of the following amino acids has a positively charged side chain at pH 7.4? -
Answer Lys
What are the products from treatment of the following peptide with trypsin? Leu-Val-
Ala-Arg-Phe-Val-Lys-Asn-Leu-Gly-Arg-Cys-Asp - Answer 1 dipeptide, 1 tripeptide, and 2
tetrapeptides
For a globular protein that is found in the cytosol of cells, _______ would most likely be
found in the proteins interior, while ________ would most likely be found on the
surface - Answer Leu; Ser
Which amino acid is generally absent from an alpha-helix? - Answer Pro
,When a cell moved along a surface, acting _______ occurs at the leading edge while
_____ occurs at the trailing edge. - Answer polymerization; depolymerization
In a muscle cell, what is the name for the bundles of myosin tails? - Answer Thick
filament
Which amino acid is critical for crosslinking of keratin fibers? - Answer Gly
The central ion of the heme group of hemoglobin is ________. - Answer Fe2+
The idea that binding of one molecule of oxygen to hemoglobin enhances further
binding of oxygen to hemoglobin is called - Answer cooperation
What explains how cell division is blocked by drugs that prevent proper microtubule
function? - Answer chromosome separate along a microtubule spindle
What explains the conversion of hemoglobin subunits from deoxy to oxy state? - Answer
All four subunits switch simultaneously
When oxygen is bound to the heme group of myoglobin, it is coordinated between
______ and ______. - Answer E7 His; Fe2+ of heme
During the formation of microfilaments, what occurs? - Answer ATP hydrolysis is
catalyzed by F-Actin
How does CO2 affect hemoglobin-oxygen binding? - Answer CO2 is converted to
bicarbonate and H+ which promotes the deoxy state
, Heme is considered a(n) ________. - Answer prosthetic group
What represents the longest distance traveled by a kinesin-vesicle complex? - Answer
movement of a neurotransmitter vesicle down the axon of a nerve cell
What allosteric effector has the greatest ability to stabilize the deoxy state of
hemoglobin? - Answer BPG
The helical structure of collagen contains ______. - Answer three left-handed helices
would around each other in a right-handed triple helix
Hemoglobin S, the variant responsible for the misshappen red blood cells characteristic
of the disease sicke-cell anemia, is potentially advantageous to heterozygotes because it
confers some level of resistance to the disease - Answer Malaria
During the initial synthesis of collagen molecules, ______ and ______ are most often
incorporated into the growing protein - Answer Gly; Pro
Which of the following best explains the ability for carbon monoxide (CO) to bind to
hemoglobin (Hb) despite the relatively low concentration of CO? - Answer CO binds to
Hb about 250 times more strongly than oxygen
Which of the following describes the sequence of events in the myosin-actin cycle? -
Answer 1. ATP binds to myosin
2. myosin release from actin
3. myosin binds to another actin subunit
4. release of Pi and ADP
5. stretched myosin returns to original formation
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