SOLUTION SMALL ANGLE XRAY SCATTERING STUDIES OF HEAT SHOCK COGNATE PROTEIN

$143,176P41FY2002RRNIH

Stanford University, Stanford CA

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Abstract

We have continued with our solution small-angle x-ray studies of the bovine 70 kDa heat shock cognate protein, primarily utilizing a 60 kDa fragment (for which the C-terminal ~100 amino acids have been removed) which is less prone to self-aggregation than the full-length protein. Our current focus is to delineate which functional groups are required for the ATP-induced conformational change by measuring the DRg of proteins with mutations in the nucleotide binding site. We are completing measurements on seven different mutants at this time.

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