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J Biol Chem. 2002 Aug 23;277(34):30968-75. Epub 2002 May 25.

Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.

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1
Department of Biochemistry, Stanford University, 279 Campus Drive West, Stanford, CA 94305,USA.

Abstract

Understanding protein conformation, interactions, and ligand binding is essential to all biological inquiry. We report a novel biochemical technique, called misincorporation proton-alkyl exchange (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 triosephosphate isomerase (beta/alpha)(8) barrel, accurately determining its substrate-binding site, a protein-protein interaction surface, the solvent-accessible protein surface, and 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.

PMID:
12185208
DOI:
10.1074/jbc.M203172200
[Indexed for MEDLINE]
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