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Bioc 384 Exam 2|| Questions And 100% Correct Answers Already Graded A+|| Latest And Complete Update With Verified Solutions Guaranteed Pass!!!

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BIOC 384 EXAM 2|| QUESTIONS AND 100% CORRECT ANSWERS ALREADY GRADED A+|| LATEST AND COMPLETE UPDATE WITH VERIFIED SOLUTIONS GUARANTEED PASS!!!

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BIOC 384 EXAM 2|| QUESTIONS AND 100%
CORRECT ANSWERS ALREADY GRADED A+||
LATEST AND COMPLETE UPDATE WITH
VERIFIED SOLUTIONS GUARANTEED PASS!!!
Which separation technique exploits the density differences of biomolecules and
organelles?


A. Dialysis using dialysis tubing in a beaker with buffer.
B. Salting out by ammonium sulfate using a beaker and stir bar.
C. Centrifugation using centrifuge tubes in a rotor placed in a centrifuge. D. An
ionic exchange column using a charge resin at an optimal pH.
E. An affinity column using a solid matrix with a specific ligand attached. -
ANSWER: C. Centrifugation using centrifuge tubes in a rotor placed in a
centrifuge.


What protein feature will cause the protein to bind to a metal in chelation affinity
chromatography—specifically, a resin with immobilized Ni2+?


. proteins with antigenic affinity for divalent cations.
B. proteins that have a heme that can bind divalent cation metals, such as iron or
nickel.
C. recombinant proteins engineered to have six histidines at the N or C terminus of
the protein.
D. proteins with a negative charge on the amino terminus and a positive charge on
the carboxyl terminus. E. proteins that bind cadmium to form a nickel-cadmium
compound similar to batteries. - ANSWER: C. recombinant proteins engineered to
have six histidines at the N or C terminus of the protein.

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Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Selectthe
correct description of what SDS does in denatured electrophoresis.


A. Because SDS is a detergent, it supports the native state by interacting with the
nonpolar portions of a protein, stabilizing the three-dimensional structure of a
protein so that it can migrate based on shape.


B. SDS forms hydrogen bonds with the carbonyl carbon and amide nitrogen of the
polypeptide backbone.


C. SDS is a charged detergent that neutralizes the protein, allowing the protein to
migrate through the gel.


D. SDS is a bivalent cation that can interact with two negatively charged carboxyl
groups at the same time.


E. SDS is an amphipathic compound that binds tothe hydrophobic portion of
proteins and give a negative
charge derived from the polar head group such that proteins have a proportional
charge to mass ratio. - ANSWER: E. SDS is an amphipathic compound that binds
tothe hydrophobic portion of proteins and give a negative
charge derived from the polar head group such that proteins have a proportional
charge to mass ratio.


Which of the experimental steps listed at the right is considered the most
challenging in X-ray crystallography?


A. Mounting the crystal on the X-ray
B. Determining the phases of the diffracted X rays

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C. Dissolving the protein in the appropriate solvent
D. Using the correct radio frequency for nuclear spin
E. Isolating epitope-tagged proteins from bacteria. - ANSWER: B. Determining
the phases of the diffracted X rays


Representative Protein
a. Telomerase
b. Protein Kinase A _
c. Actin polymer ____
d. Lactose permease ____
e. Hexokinase


Major Protein Class
1. Cell signaling
2. Transport protein
3. Genomic caretaker
4. Structural protein
5. Metabolic enzyme


A. 5, 3, 2, 1, 4
B. 3, 5, 4, 2, 3
C. 3, 4, 1, 5, 2
D. 3, 1, 4, 2, 5
E. 1, 3, 2, 4, 5 - ANSWER: D. 3, 1, 4, 2, 5

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