Exam 2 Qs

1. 1what is this molecule?

   

   1. Aglucose
   2. B2-mercaptoethanol or beta-mercaptoethanol
   3. Ccysteine
   4. Dmethionine
   5. Eethanol
2. 2What is the function of this molecule?

   

   1. Asmell bad
   2. Bprovide energy
   3. Cblock protein synthesis
   4. Dreduce (break) disulfide bonds
   5. Einhibit bacterial growth
3. 3Which of the following 'assays' would be most specific for a particular protein?

   1. ABradford assay
   2. BUV absorptivity
   3. CRadioimmunoassay
   4. Dmolar absorptivity
   5. Eamino acid analysis
4. 4An enzyme-linked immunosorbent assay requires

   1. Aa radioactive substrate
   2. Ba radioactive standard for binding to the antibody
   3. Caromatic amino acids
   4. Dan antibody that binds the protein of interest
   5. Ea catalytic antibody
5. 5Which physical characteristics is not commonly used in protein separation?

   1. ASolubility
   2. BStereochemistry
   3. CSize
   4. DCharge
   5. EPolarity
6. 6Adding additional salt to a protein solution can cause:

   1. Aan increase in solubility called 'salting in'
   2. Ba decrease in solubility called 'salting out'
   3. Cprotein precipitation from solution
   4. Dall of the above
   5. Enone of the above
7. 7Which of the following amino acids would be LAST to elute at pH 8.0 from an anion-exchange column?

   1. Alysine
   2. Balanine
   3. Cglutamic acid
   4. Dasparagine
   5. Eglycine
8. 8Which of the following amino acids would be FIRST to elute at pH 8.0 from an anion-exchange column?

   1. Alysine
   2. Balanine
   3. Cglutamic acid
   4. Dasparagine
   5. Eglycine
9. 9The pK1, pK2, and pKR of the aa lysin is 2.2, 9.1, and 10.5 respectively. The pK1, pK2, and pKR of the amino acid arginine are 1.8, 9.0, 12.5, respectively.
   A student at SDSU wants to use ion-exchange chromatography to separate lysine from arginine. What pH is likely to work best for this separation?

   1. A1.5
   2. B2.5
   3. C5.5
   4. D7.5
   5. E10.5
10. 10If you were to mutate 6 aa positions in a protein such that all aa are represented at each of the three sites, how many different proteins would you generate

    1. A4096
    2. B8000
    3. C1048576
    4. D160000

11. 11The salting in of proteins can be explained by

    1. Asalt ions reducing the polarity of the solution
    2. Bsalt ions increasing the hydrophobic interactions
    3. Creleasing hydrophobic proteins from nonpolar tissue environments
    4. Dhydration of the salt ions reducing the solubility of proteins
    5. Esalt counter-ions reducing electrostatic attractions between protein molecules
12. 12The quantification of protein due to their absorbance at ~280nm (UV region) is due to the large absorptivity of the ____ aa.

    1. Aanionic
    2. Bdansylated
    3. Ccleaved
    4. Dpolar
    5. Earomatic
13. 13Which of the following is the correct definition for the primary structure of a protein?

    1. Ait corresponds to the linear sequence of aa
    2. Bit consists of alpha helices, beta sheets, and turns
    3. Cit describes the final 3-d structure of a protein
    4. DIt describes the number of units that a protein consists of
    5. Enone of the above
14. 14Which of the following is the correct definition for the secondary structure of a protein?

    1. Ait corresponds to the linear sequence of aa
    2. Bit consists of alpha helices, beta sheets, and turns
    3. Cit describes the final 3-d structure of a protein
    4. DIt describes the number of units that a protein consists of
    5. Enone of the above
15. 15Which of the following is the correct definition for the tertiary structure of a protein?

    1. Ait corresponds to the linear sequence of aa
    2. Bit consists of alpha helices, beta sheets, and turns
    3. Cit describes the final 3-d structure of a protein
    4. DIt describes the number of units that a protein consists of
    5. Enone of the above
16. 16Which of the following is the correct definition for the quaternary structure of a protein?

    1. Ait corresponds to the linear sequence of aa
    2. Bit consists of alpha helices, beta sheets, and turns
    3. Cit describes the final 3-d structure of a protein
    4. DIt describes the number of units that a protein consists of
    5. Enone of the above
17. 17A fast and common method for determining the protein concentration in column effluent is

    1. Atandem mass spectrometry
    2. Bsalting in with ammonium sulfate
    3. Cdrying a portion and weighing the solid
    4. Dmeasuring light absorption at 280 nm
    5. EEdman degradation

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Chem 365 Quiz sobre Exam 2 Qs, criado por Crisila A em 05-11-2020.

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Crisila A

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