William Wedemeyer
Assistant Professor

• Ph.D. 1998, Cornell University
• Postdoctoral Fellow 1998-2001, Cornell University
• Postdoctoral Fellow 2001-2003, University of Washington, Seattle

proteins@msu.edu
509 Biochemistry Building
Michigan State University
East Lansing, MI 48824-1319
Office: 517-355-6490

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William Wedemeyer

Research Interests

The Wedemeyer lab combines computational and experimental methods to answer important biological questions about protein structure. Our principal focus is gp120 (the envelope protein of HIV) but we are also pursuing basic research about the physics of protein folding using peptides and small proteins. Our software is protected by the GNU Public License.

Conformational Changes in gp120 During HIV-1 Cell Entry

HIV is perhaps the most critical public health problem of our time, with roughly 40 million people infected and roughly 10,000 deaths per day. The HIV envelope protein, gp120, is the principal target for vaccines and antibody neutralization, being the sole exposed viral protein. However, gp120-based vaccines have not been successful and relatively few anti-gp120 antibodies are effective at neutralizing the virus; of these few antibodies, none are effective against all forms of the virus. MORE

Computational Protein Structure Prediction/Design

The methods of computational protein structure prediction have matured in recent years, so that the structure of individual domains can be predicted de novo (i.e., from the amino-acid sequence alone) within 3-5 Å CA rmsd. Nevertheless, these methods are prone to fail if the domain is unusually large (>150 residues), has poorly predicted secondary structure, or has a high fraction of long-range contacts. Moreover, there are no reliable methods for refining approximately correct structures (e.g., 5 Å CA rmsd to native) to higher resolution (e.g., 3 Å CA rmsd). We are developing new sampling methods and force-fields to overcome these obstacles.

Experimental Studies of Protein/Peptide Electrostatics

Successful protein prediction and design requires accurate energy functions for scoring trial conformations. Unfortunately, the electrostatic component of present-day energy functions seems to be inaccurate; this is especially problematic, since the electrostatic component is long-ranged. We are studying the electrostatics of peptides and proteins experimentally in an effort to improve these potential functions.

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