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Dr. Grayson Snyder

Associate Professor
Cooke 513
phone: (716) 645-4939
e-mail: gsnyder@buffalo.edu
Further research info

Research Summary

The structures of many naturally occurring enzyme inhibitors, toxins, and hormones include a small rigid tightlycrosslinked disulfiderich polypeptide mainframe. By chemical synthesis of mutants, computer modeling, nmr spectroscopy, and analysis of disulfide pair formation, we are determining factors responsible for the folding of conotoxin (a snail toxin), apamin (a bee venom toxin), and endothelin (a human hormone). The latter two of these small disulfide rich proteins have four cysteines at identical positions in the primary sequence, but those cysteines pair with each other to make different sets of disulfides. The specific aim of this research is to develop a rational approach for engineering and designing new proteins capable of regulating human diseaserelated processes.

Selected Publications

• Zhang, R. and Snyder, G.H. (1990) Factors Governing Selective Formation of Specific Disulfides in Synthetic Variants of Conotoxin (submitted)
• Snyder, G.H., Zhang, Y.H., Xiao, Z.S., Zhang, R., Hammarskjold, M.L., and Rekosh, D.M. (1990) A Bacterially Produced CD4Binding Domain of the HIV1 Envelope Protein (submitted)
• Zhang, R. and Snyder, G.H. (1989) Dependence of Formation of Small Disulfide Loops in TwoCysteine Peptides on the Number and Types of Intervening Amino Acids. J. Biol.Chem. 264: 18472-18479