Professor Akio Maeda
Department of Biophysics
Kyoto University
Japan

Wednesday, November 19, 1997
3:00 pm (CT)
3269 Beckman Institute

Abstract

FTIR is one of the most powerful tools to detect changes in the chemical bonds involved in the functional process of light activatable proteins like bacteriorhodopsin and rhodopsin. Detected changes can be assigned to specific residues by use of relevant isotope labeling and site specific mutant proteins. We are mainly concerned on the signals for water, peptide backbone and carboxylic acid. I would like to talk about three topics from our studies. (1) Water structural changes in a swtiching reaction through L, M and N intermediates of bacteriorhodopsin. (2) A structural feature in the trans-membrane region of bovine rhodopsin. (3) Interaction of photoactivated bovine rhodopsin with G-protein.

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