Role of Aspartate in the Catalytic Diad

Werneburg, Brian G.

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 #: 1F32GM015973-01
• Application #: 2170472
• Study Section: Biomedical Sciences Study Section (BIOM)
• Project Start: 1994-01-23
• Budget Start: 1993-12-01
• Budget End: 1994-11-30
• Support Year: 1
• Fiscal Year: 1993

Institution

• Name: Ohio State University
• Department: Chemistry
• Type: Schools of Arts and Sciences
• DUNS #: 098987217
• City: Columbus
• State: OH
• Country: United States
• Zip Code: 43210

Publications

Ahn, J; Kraynov, V S; Zhong, X et al. (1998) DNA polymerase beta: effects of gapped DNA substrates on dNTP specificity, fidelity, processivity and conformational changes. Biochem J 331 ( Pt 1):79-87

Ahn, J; Werneburg, B G; Tsai, M D (1997) DNA polymerase beta: structure-fidelity relationship from Pre-steady-state kinetic analyses of all possible correct and incorrect base pairs for wild type and R283A mutant. Biochemistry 36:1100-7

Zhong, X; Patel, S S; Werneburg, B G et al. (1997) DNA polymerase beta: multiple conformational changes in the mechanism of catalysis. Biochemistry 36:11891-900

Kraynov, V S; Werneburg, B G; Zhong, X et al. (1997) DNA polymerase beta: analysis of the contributions of tyrosine-271 and asparagine-279 to substrate specificity and fidelity of DNA replication by pre-steady-state kinetics. Biochem J 323 ( Pt 1):103-11

Werneburg, B G; Ahn, J; Zhong, X et al. (1996) DNA polymerase beta: pre-steady-state kinetic analysis and roles of arginine-283 in catalysis and fidelity. Biochemistry 35:7041-50