Conformational Transitions of the Reca Protein

Stole, Einar

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Postdoctoral Individual National Research Service Award (F32)
• Project #: 1F32GM016284-01
• Application #: 2170749
• Study Section: Biomedical Sciences Study Section (BIOM)
• Project Start: 1994-03-14
• Budget Start: 1993-09-15
• Budget End: 1994-09-14
• Support Year: 1
• Fiscal Year: 1993

Institution

• Name: Johns Hopkins University
• Department: Biochemistry
• Type: Schools of Public Health
• DUNS #: 045911138
• City: Baltimore
• State: MD
• Country: United States
• Zip Code: 21218

Publications

Stole, E; Bryant, F R (1997) The rate-determining step on the recA protein-catalyzed ssDNA-dependent ATP hydrolysis reaction pathway. Biochemistry 36:3483-90

Stole, E; Bryant, F R (1996) Reengineering the nucleotide cofactor specificity of the RecA protein by mutation of aspartic acid 100. J Biol Chem 271:18326-8

Stole, E; Bryant, F R (1995) Spectroscopic demonstration of a linkage between the kinetics of NTP hydrolysis and the conformational state of the recA-single-stranded DNA complex. J Biol Chem 270:20322-8