Background Ivan Rayment, Ph.D., is the Michael G. Rossmann Professor of Biochemistry in the Department of Biochemistry at the University of Wisconsin-Madison. Understanding how proteins function at the molecular level, which typically starts with the determination of a three-dimensional structure by X-ray crystallography, is a common research theme in Professor Rayment’s laboratory. His research lab was the first to solve the structure of myosin, which is the major motor protein in muscle. X-ray crystal structures determined by his research group have been featured on the cover of journals such as Science, Nature, and Biochemistry. Rayment has authored more than 220 publications. He was former co-director of the Institute for Enzyme Research. In addition, he is a Fellow of the American Association for the Advancement of Science and of the Biophysical Society. Rayment received his Ph.D. in chemistry from Durham University in England.

The Arnold C. Ott Lectureship in Chemistry was created and endowed by a generous gift from Dr. Arnold C. Ott and Marion Ott. Dr. Ott received his Ph.D. in 1943 from Michigan State University in Chemistry/Physics/Bacteriology and is a leading chemist and entrepreneur in West Michigan. He is one of the co-founders of Grand Valley State University and served on the GVSU Board of Trustees for 28 years.

Public Lecture

Cancelled due to coronavirus pandemic. Please check back for rescheduled dates.

Location: Grand River Room, Russel H. Kirkhof Center, Allendale Campus

Parking:  For free parking during Thursday evening's public lecture, you can obtain a visitor's parking pass by contacting Dave Leonard

Title: Myosin: How Simple Chemistry Leads to Directed Movement and Beyond

Abstract:  Directed movement is a hallmark of life. In humans and other animals this manifests itself most clearly as the ability to walk, run, or fly, all of which are driven by muscle contraction. The question of how this is accomplished has been the subject of enquiry since at least 1100 AD. It was not until 1859, however, that the major muscle protein myosin was isolated and not until 1939 that it was shown to hydrolyze ATP. Since then the major questions have centered on how the hydrolysis of a single phosphoester bond leads to movement of at least 10 nm and how the chemical energy is transferred into work in a controlled biological setting. From any viewpoint this is a truly remarkable phenomenon. This lecture will focus on the manner in which this is accomplished at the molecular level in the context of simple chemistry. Efforts by many investigators over the past 27 years have generated a robust structural framework for understanding myosin-based molecular motors. In turn this has proven invaluable in the development of new pharmacological agents that promise to ameliorate many forms of heart disease.

Chemistry Seminar

Cancelled due to coronavirus pandemic. Please check back for rescheduled dates.

Location: Pere Marquette Room, Russel H. Kirkhof Center, Allendale Campus

Parking:  For free parking during Friday's Chemistry seminar, you can obtain a visitor's parking pass by contacting Dave Leonard

Title:  Structural Studies of the Yeast Microtubule Organizing Center: Taming the Coiled Coil

Abstract:  Centrosomes and spindle pole bodies (SPBs) are large membrane-less organelles that serve as microtubule-organizing centers (MTOCs), forming the poles of the mitotic spindle and positioning the nucleus during cell division. They also function as signaling platforms by concentrating cell cycle regulators and other factors. Despite the morphological diversity between centriolar-based centrosomes and plaque-like SPBs, such as those found in the budding yeast Saccharomyces cerevisiae, over half of all SPB components have a direct ortholog found in centrosomes. Thus, study of the SPB in yeast provides a route to understanding centrosomes found in higher organisms. The goal of this work is to establish a molecular framework for the budding yeast SPB.

MTOCs are massive macromolecular assemblies built from multiple copies of numerous proteins. Many of these proteins incorporate sections of coiled coil that connect interacting domains within the assembly. Although at first sight coiled coils are simple structural motifs, studies of the associated domains have often proved difficult because removal of the intervening coiled coil frequently yields aggregated or insoluble protein. This problem has been solved for many proteins by including a folding domain, where the most commonly used assembly domain is the ~30 amino acid residue long leucine zipper from the GCN4 transcription factor. Unfortunately, the leucine zipper approach yields a highly asymmetric construct that is often unsuitable for structural investigations. We have solved this problem by incorporating small globular fusion domains, which has allowed heterologous expression and purification of all of the central components of the S. cerevisiae SPB and in some cases the determination of high-resolution X-ray structures. Our strategy has also facilitated studies on myosin, tropomyosin, and kinesin and is generally applicable to proteins that contain coiled coils. My lecture will describe our structural and functional studies on the yeast SPB and the prospect of a high-resolution structure of the intact assembly.

Vernon Ehlers, Ph.D.
U.S. Congress

Michael D. Parker, M.B.A.
Dow Chemical Company

Carl Djerassi, Ph.D.
Stanford University

Robin D. Rogers, Ph.D.
University of Alabama

Virginia W. Cornish, Ph.D.
Columbia University

Richard N. Zare, Ph.D.
Stanford University

Thomas H. Lane, Ph.D.
Dow Corning Corporation

Chad A. Mirkin, Ph.D.
Northwestern University

Gregory A. Petsko, Ph.D.
Brandeis University

Harry B. Gray, Ph.D.
California Institute of Technology

Gary M. Hieftje, Ph.D.
Indiana University

Roderick MacKinnon, M.D.
Nobel Laureate in Chemistry
The Rockefeller University

Kevan Shokat, Ph.D.
University of California, San Francisco

Ada Yonath, Ph.D.
Nobel Laureate in Chemistry
Weizmann Institute of Science

W. Carl Lineberger, Ph.D.
University of Colorado, Boulder

Richmond Sarpong, Ph.D.
University of California, Berkeley

Jeffrey Moore, Ph.D.
University of Illinois, Urbana-Champaign

Wilson Ho, Ph.D.
University of California, Irvine

Geraldine Richmond, Ph.D.
University of Oregon

Sara E. Skrabalak, Ph.D.
Indiana University

Thomas J. Meyer, Ph.D.
University of North Carolina, Chapel Hill

Brian K. Shoichet, Ph.D.
University of California, San Francisco

Daniel M. Neumark, Ph.D.
University of California, Berkeley

Stephen L. Buchwald, Ph.D.
Massachusetts Institute of Technology

Melanie Sanford, Ph.D.
University of Michigan

Karen Trentelman, Ph.D.
Getty Conservation Institute