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Biochemistry  3G03                            Test  3                            October  28,  2013    

Note:  Please  check  your  examination  booklet  to  ensure  all  pages  are  there.  There  are  27  questions   and  7  pages.  Please  mark  your  answers  clearly  on  the  examination  answer  sheet.  You  can  keep  the   examination  booklet.  There  are  several  different  versions  of  this  test,  therefore  it's  important  that   you  mark  your  version  on  the  CLASSROOM  ANSWER  SHEET  (scantron)  according  to  question  1  &  2.  

 

Please  also  mark  your  seat  number  on  the  scantron  in  the  space  for  RECORD  (SEAT)  NUMBER   according  to  the  following  table.  

 

Failure  to  indicate  your  version  number  or  seat  number  may  result  in  5%  penalty.  

 

Table  for  conversion  of  ROW  number:  

A   01   F   06   K   11   P   16   U   21   Z   26   B   02   G   07   L   12   Q   17   V   22  

C   03   H   08   M   13   R   18   W   23   D   04   I   09   N   14   S   19   X   24     E   05   J   10   O   15   T   20   Y   25    

First  two  numbers  in  RECORD  (SEAT)  NUMBER  are  used  for  letter  (row)  and  the  following  three   numbers  are  for  the  seat  number.    For  example:  w020  is  23020.  

________________________________________________________________________________________________________________  

 

1. Please mark question 1 c 2. Please mark question 2 a

3. When oxygen is bound to the heme group of myoglobin, it is coordinated between _____ and _____.

a) E7 His; Fe2+ of heme b) E7 His; Fe3+ of heme c) none of the rest d) F8 His; Fe2+ of heme e) F8 His; Fe3+ of heme

4. During the initial synthesis of collagen molecules, _____ and _____ are most often incorporated into the growing protein.

a) Ser; Pro b) Ala; Gly c) Pro; Ala d) Ser; Gly e) Gly; Pro

5. Which of the following fibers is correctly paired with the protein that forms the fiber?

a) microfilaments: actin

b) extracellular support fibers: collagen c) intermediate filaments: keratin d) microtubule: tubulin

e) all of the rest

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6. What amino acid performs the nucleophilic attack during the chymotrypsin mechanism?

a) Lys b) Ser c) His d) Asp e) Thr

7. How does a catalyst affect the overall delta-G of an endergonic reaction?

a) the reaction becomes exergonic b) it has no effect

c) none of the rest

d) the reaction becomes more endergonic e) the reaction has a delta-G of zero

8. Which allosteric effector has the greatest ability to stabilize the deoxy state of hemoglobin?

a) H+

b) BPG c) O2 d) CO2

e) all of the rest have equal ability

9. The idea that binding of one molecule of oxygen to hemoglobin enhances further binding of oxygen to hemoglobin is called _____.

a) allosterism b) none of the rest c) cooperativity d) fractional saturation e) homologous binding

10. The isoelectric point of the peptide RTRADAE is?

a) 3.00 b) 6.53 c) 3.98 d) 10.74 e) 10.21

11. With respect to oxygen saturation, hemoglobin is _____ saturated at the pO2 of the lungs and _____

saturated at the pO2 of the tissue a) 20%; 20%

b) 50%; 20%

c) >90%; between 30 and 70%

d) 50%; between 30 and 70%

e) 25%; 20%

12. What three amino acids are found in the catalytic triad of chymotrypsin?

a) Cys, Lys, Glu b) Glu, His, Thr c) Asp, His, Ser d) Asn, His, Thr e) Ser, Arg, Cys

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13. How does CO2 affect hemoglobin-oxygen binding?

a) CO2 binds directly to the oxygen binding site, displacing oxygen and thus promoting the deoxy state b) CO2 displaces BPG, thus promoting the oxy state

c) none of the rest

d) CO2 is converted to bicarbonate and H+ which promotes the oxy state e) CO2 is converted to bicarbonate and H+ which promotes the deoxy state

14. Which of the following occurs in hemoglobin upon oxygen binding?

a) hemoglobin changes from the R state to the T state

b) the heme Fe2+ is pulled out of the plane of the heme group

c) the His coordinated to the heme Fe2+ is pushed away from the heme group d) the central cavity between the four subunits is decreased in size

e) all of the rest occur

15. A plot of the binding of oxygen to myoglobin as a function of pO2 gives a _____ shape; a similar plot for hemoglobin gives a _____ shape.

a) sigmoidal; hyperbolic b) hyperbolic; hyperbolic c) hyperbolic; exponential d) sigmoidal; sigmoidal e) hyperbolic; sigmoidal

16. Why is the decreased affinity of fetal hemoglobin for BPG advantageous to the fetus?

a) More free BPG is available to bind to adult hemoglobin, resulting in a shift of adult hemoglobin to the R state

b) It reduces fetal hemoglobin's P50

c) With fewer BPG molecules bound there are more heme residues available for O2 binding d) Decreased BPG binding biases the fetal hemoglobin toward the T state

e) BPG is available to bind to fetal myoglobin, helping to release O2 in fetal muscle tissue

17. In the chymotrypsin mechanism, what is used to stabilize the negative charge on the carbonyl oxygen of the transition state?

a) electrostatic interaction of the positively charged His and carbonyl oxygen b) all of the rest

c) electrostatic interaction of the active site Zn2+ and carbonyl oxygen d) electrostatic interaction of the negatively charged Asp and carbonyl oxygen e) hydrogen bonding between the enzyme and the anion from the carbonyl oxygen

18. In the enzyme catalyzed decarboxylation of acetoacetate, a Schiff base is formed between the ketone of acetoacetate and a _____ residue in the active site of the enzyme.

a) Arg b) Asn c) Ser d) Lys e) Glu

19. Which of the following statements does not apply to collagen?

a) One single polypeptide forms a left-handed helix.

b) It contains hydroxylated amino acids.

c) Glycine at every third position is essential for the stability of the triple helical structure.

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e) The triple helical structure twists in the right-handed direction.

20. Hemoglobin is 50% saturated with oxygen when pO2 = 26 torr. If hemoglobin exhibited hyperbolic binding (as myoglobin does) with 50% saturation at 26 torr. Which of the following statements is correct?

(pO2 =100 in the lungs and pO2 = 30 in the tissues; fractional saturation YO2 = pO2 / {K + pO2} and K=p50=pO2 when YO2=0.5)

a) The fractional saturation when pO2 = 100 torr is 0.59 b) None of the rest

c) The fractional saturation when pO2 = 30 torr is 0.24 d) Hemoglobin is fully oxidized in the tissues

e) Hemoglobin can only use approximately 1/4 of its capacity to deliver O2 to the tissues

21. EcoRI recognizes the sequence 5'-G|AATTC-3' ("|" indicates the point of cleavage). Treatment of the following oligonucleotide with EcoRI would produce two oligonucleotides with sizes of _____ double- stranded nucleotides containing _____ ends.

5'-GAAGTCGATACAGAATTCGTACCTAGC-3' a) 13 and 10; sticky

b) 11 and 8; sticky c) 12 and 13; blunt d) 12 and 9; sticky e) 12 and 8; blunt

22. Of all the species that enzymes bind, they are thought to bind most tightly to _____.

a) substrates b) products c) transition states

d) all are bound very tightly e) intermediates

23. Which of the following is an example of a conservative amino acid substitution?

a) Asp -> Gln b) Ile -> Leu c) Arg -> Cys d) Phe -> Tyr e) Ser -> Glu

24. Which of the following explains the conversion of hemoglobin subunits from deoxy to oxy state?

a) each subunit switches only upon oxygen binding to the particular subunit b) both beta subunits simultaneously switch first followed by both alpha subunits c) all four subunits switch simultaneously

d) both alpha subunits simultaneously switch first followed by both beta subunits e) none of the rest

25. In an enzyme mechanism that generates a negative charge in the transition state, which of the following would be most effective to have in the active site of the enzyme?

a) transition metal anion b) transition metal cation c) none of the rest d) Asp residue e) Gln residue

(5)

26. Which protein in the blood is responsible for converting fibrinogen to fibrin?

a) factor VIIa b) factor X c) thrombin d) factor VII e) prothrombin

27. Zymogens are not enzymatically active because _____.

a) the pH of their environment is not optimal for activity

b) their active sites are distorted and incapable of enzymatic activity c) none of the rest

d) they do not contain the cofactors required for catalysis e) they are the product of mutated genes

THE END of QUESTIONS  

 

Fig 1. The oxygen binding site in myoglobin

Fig 2. Oxygen binding to hemoglobin

Conformation of oxyhemoglobin - R state; oxy state;

Conformation of deoxyhemoglobin - T state; deoxy state;

Fig 3. Decarboxylation of Acetoacetate

 

   

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Fig 4. Oxygen transport and the Bohr

effect Fig 5. The Coagulation Cascade

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Fig 6. The catalytic mechanism of chymotrypsin and other serine proteases

End  of  Data  

Figure

Table	
  for	
  conversion	
  of	
  ROW	
  number:	
  
Fig 1. The oxygen binding site in  myoglobin
Fig 4. Oxygen transport and the Bohr
Fig 6. The catalytic mechanism of chymotrypsin and other serine proteases

References

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