Most recently, DAVID W. CRAIG, Ph.D. has directed with professor Weseley Perkins the Hobart and William Smith Colleges Alcohol Education Project a collection of educational and research initiatives about alcohol, tobacco, and other drug use in youthful populations. He also directs a program of research that monitors late night blood alcohol concentrations of college students at HWS. He is a leader in interdisciplinary program development particularly in the integration of the sciences into programs focusing on health and wellness at both the college and secondary school levels and has published numerous publications and a recent film on this subject. He is a developer with colleague Wesley Perkins of Campus Factoids™ electronic media resources for social norms prevention campaigns as well as the Social Norms Surveys Online from HWS and has promoted these strategies nationally at workshops for secondary schools and higher education nationwide. Their Alcohol Education Project recently developed a very successful program for intercollegiate athletes and received one of the first "Model Program" grant recognition awards presented by the U. S. Department of Education.
Earlier research has been directed toward the elucidation of enzyme catalytic mechanism and the means by which the biological activity of a protein can be regulated by small molecules. My dissertation research at the University of California, Riverside, was directed toward the study of a-ketoglutarate dehydrogenase complex from cauliflower. This enzyme is of biological interest because it is a multienzyme complex and is allosteric by virtue of the fact that it is activiated by AMP. The problem has been approached with both steady-state and presteady-state kinetic analyses, kinetic isotope effect experiements, and comparative fluorescent activator analog studies. These experimental approaches have yielded much insight into the mode of AMP activation and its catalytic mechanism.
Professor Craig's postdoctoral work involved investigations of the regulatory mechanism of rabbit muscle phosphofructokinase in the laboratory of Dr. Gordon G. Hammes at Cornell University, Department of Chemistry. The enzyme has one catalytic site and three reulatory sites per subunit. The catalytic site binds ATP-Mg +2 and fructose-6-phosphate and the regulatory sites bind cAMP, ATP, and citrate, respectively. My approach to this problem has been to determine the structural interrelationships between the catalytic and regulatory sites by measuring the distrances between them with fluorescence energy transfer techniques. This involves designing reagents which bind covalently to specific sites on the enzyme and which possess the required absorbance and fluorescence spetroscopic properties. Several distances have been measured in this manner indicating that interacting binding sites are separated by 30 to 40 A. I am continuing this work at Hobart and William Smith Colleges in the Department of Chemistry.
In the summer of l984 Professor Craig began a collaboration with Professor Bart Fiori at the New York State Agricultural Experiment Station in Geneva, N. Y. We are investigating the chemical mechanism for Birch leaf minor resistance in Birch Tres. We have found four resistant varieties of birch and are characterizing the biochemical differences between these and susceptible varieties. This research was extended to the study of flea beetle resistance in solanum species.
Finally, Professor Craig developed computer modeling software for the display and study of Brookhaven National Laborotory Protein Data Bank crystal structure files and the analysis of peptide conformation through nuclear magnetic resonance and computational simulation. This software is currently used in support of biochemical coursework and research at HWS.