6. The highest structural complexity of insulin is best described by its: A. Pri

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6. The highest structural complexity of insulin is best described by its: A. Primary structure B. Secondary structure C. Tertiary structure D. Quaternary structure E. Gene encoding it 7. What is the minimum number of Cys residues found in insulin? A. 2 B. 3 C. 4 D. 6 M 1cm Measuring the UV-Vis absorption of the isolated A chain of insulin gave a signal at 280 nm and e 2800 Given the molar absorptivity value Phe (e200 M em '), Tyr (e l 400 '), and Trp ( the following is consistent with the observation? 8. 5600 M Cm'i), whicl A. It has a phenylalanine residue as it absorbs at 280 nm. B. It may have either a Tyr or a Trp residue as it absorbs 280 nm. C. It has two Tyr residues. D. It has a Trp residue at its C-terminus. E. It has a Trp residue at its N-terminu 9. Insulin was analyzed via SDS PAGE, predict which reagents may have been added to lanes 4 and 5: A. -mercaptoethanol was added to lane 5 only. B. ß-mercaptoethanol was added to both lanes 4 and 5. C. ß-mercaptoethanol was added to lane 4 only. D. Lane 5 is a mixture of periproinsulin and insulin, and lane 4 is periproinsulin. E. Lane 5 is a mixture of signaling peptide and insulin, and lane is the proinsulin. 10. Which lane on the gel is likely to correspond to periproinsulin? Lane# 1 2 3 4 5 A. 1 B. 2 C. 3 D. 4 E.5

Explanation / Answer

6. tertiary structure

7. D. 6 Cys residues take part in sulfide bond formation. There are 2 sulfide bonds between B and B chains and 1 in the A chain. Hence total 6 Cys residues are present.

8. C

9. E

10. 4th lane

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