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Papers In Press, published online ahead of print May 25, 2002
J. Biol. Chem, 10.1074/jbc.M203172200
Submitted on April 3, 2002
Revised on May 17, 2002
Accepted on May 25, 2002

MPAX: Rapid mapping of protein structure, interactions, and ligand binding

Joshua A. Silverman and Pehr B. Harbury

Department of Biochemistry, Stanford University, Palo Alto, CA 94305

Corresponding Author: harbury{at}cmgm.stanford.edu

Understanding protein conformation, interactions and ligand binding is essential to all biological inquiry. We report a novel biochemical technique, called MPAX, that can be used to footprint protein structure at single amino-acid resolution. MPAX exploits translational misincorporation of cysteine residues to generate probes for physical analysis. We apply MPAX to the TIM (beta /alpha )8 barrel, accurately determining its substrate binding site, a protein-protein interaction surface, the solvent-accessible protein surface, and for the first time, the stability of the barrel. Because MPAX requires only microgram quantities of material and is not limited by protein size, it is ideally suited for proteins not amenable to conventional structural methods, such as membrane proteins, partially folded or insoluble proteins, and large protein complexes.


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