Professor George N. Phillips, Jr.
Department of Biochemistry and Cell Biology
Rice University
Houston, TX

Friday, December 13, 1996
2:00 pm (CT)
3269 Beckman Institute

Abstract

Myoglobin continues to be studied, both as a model system for protein dynamics and for the practical design of hemoglobin-based blood substitutes. X-ray crystallography, various spectroscopies, and molecular dynamics simulations are coming together to produce remarkably detailed descriptions of ligand binding and unbinding as well as the stability of the protein against oxidation and unfolding. The basis of the specificity for oxygen over carbon monoxide has been revealed (most textbooks are wrong) and the role of electrostatics in ligand binding calculated. Low temperature and nano-second time-resolved crystallography have also revealed the structures of key intermediates in the process. The overall dynamics have also been studied and new methods of analysis reveal global as well as local substates. This understanding is being translated to protein engineering of hemoglobin for cell-free blood substitutes.

Tea and coffee will be served in R3151 Beckman Institute at 2:15pm.