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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-23
Application #
6586805
Study Section
Project Start
2002-03-01
Project End
2003-02-28
Budget Start
Budget End
Support Year
23
Fiscal Year
2002
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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