Research Interests

Most of my work as a biophysical chemist has been on membranes and ribosomes. In early studies, I developed structural evidence for the existence of lipid bilayers in membranes and for the molecular nature of the membrane lipid phase transition. Later, with Peter Moore, I helped develop the use of neutron scattering to determine the arrangement of proteins in the small ribosomal subunit from E. coli. But my major interest in recent years has been to understand and apply the principles that govern the folding and function of membrane proteins. Many membrane proteins traverse the lipid bilayer with alpha helices. Members of my laboratory and other collaborators have contributed to the development and testing of the idea that such helices can be independently stable and that a major component of folding is the side-to-side interaction of helical domains. This view has led us to a number of studies of interacting helices in lipid environments, with the result that we now believe that detailed packing interactions between helices are a major determinant of membrane protein folding, and that changes in the structural relationships between helices can provide functional mechanisms.

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Primary Section

Section 29: Biophysics and Computational Biology

Secondary Section

Section 22: Cellular and Developmental Biology