Professor Donald Engelman
Department of Molecular Biophysics & Biochemistry
Yale University
New Haven, Connecticut

Monday, February 12, 2001
3:00 pm (CT)
3269 Beckman Institute

Abstract

Transmembrane helices in polytopic proteins are well predicted by a model that treats them as single hydrophobic spans of a lipid bilayer, yet most have more contacts with other helices than with lipid. It therefore appears that one can treat each helix as a stable domain in terms of the energies of folding and oligomerization: hydrophobic interactions and main chain H-bonds stabilize individual helix domains, other energies cause the helices to interact to form larger structures. We have explored a wide range of experimental approaches to understand the chemistry of helix interactions, including mutagenesis, modeling, NMR, centrifugation, and Genetics.The results and implications of these studies will be discussed.

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