Elementary Steps in Enzyme Catalysis

Bolen, David W.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 7R01GM022300-17
• Application #: 3271083
• Study Section: Molecular and Cellular Biophysics Study Section (BBCA)
• Project Start: 1978-09-01
• Project End: 1994-05-31
• Budget Start: 1993-02-01
• Budget End: 1993-05-31
• Support Year: 17
• Fiscal Year: 1992

Institution

• Name: University of Texas Medical Br Galveston
• Type: Schools of Medicine
• DUNS #: 041367053
• City: Galveston
• State: TX
• Country: United States
• Zip Code: 77555

Publications

Yao, M; Bolen, D W (1995) How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry 34:3771-81

Huang, Y; Bolen, D W (1993) Covalent bond changes as a driving force in enzyme catalysis. Biochemistry 32:9329-39

Senear, D F; Bolen, D W (1992) Simultaneous analysis for testing of models and parameter estimation. Methods Enzymol 210:463-81

Bolen, D W; Slightom, J L (1990) Calorimetric determination of linkage effects involving an acyl-enzyme intermediate. Biophys Chem 37:303-12

Santoro, M M; Bolen, D W (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8

Bolen, D W; Santoro, M M (1988) Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle. Biochemistry 27:8069-74

Bolen, D W; Kimura, T; Nitta, Y (1987) Energetics of alpha-chymotrypsin-mediated hydrolysis of a strained cyclic ester. Biochemistry 26:146-53