Dr. Terry L. Helser, Professor of Chemistry
227 Physical Sciences Building, Oneonta, NY 13820-4015
Phone: (607)436-3518 or Email to:
Study Guide - Biochemistry, The Molecular Basis of Life, 4th Ed., 2009, T. & J.R. McKee (Oxford Univ. Press)
Chapter 5: The Three-Dimentional Structure of Proteins

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Which amino acid(s) forms disulfide bridges? What is their importance?

How would you write the complete name for the Leu enkephalin structure? (page 74)

List and give examples of the major functions of proteins.

Define primary (1°), secondary (2°), tertiary (3°) and quaternary (4°) structures in proteins.

What are the two major types of 2° structures? Which has parallel and antiparallel forms, and what are they? Of what 2° structure is collagen made? What are supersecondary structures?

What is meant by the terms native conformation and denaturation ? What conditions and reagents cause a protein to denature? Why, in each case?

Biochemical Methods chapter 5.4, p. 122f: How is amino acid composition of a peptide determined? Why is this important?

How is the primary structure of a peptide determined? How are N-terminal and C-terminal amino acids determined? What technique has been automated in the "sequenator"? Which reagents specifically cleave proteins into peptides, and what amino acid will be on the C-end of each fragment? How are fragments aligned to give the full sequence?

What techniques are used to determine 3° and 4° structures? Give an example of each.

End of chapter review questions 1. 2. 5. 6. 7. 9. 14. 15. 19. 21. 22. 24. 27.-34. 37. 38. 42. 55.

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