Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM048358-03
Application #
2185833
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1994-08-01
Project End
1998-07-31
Budget Start
1996-08-01
Budget End
1998-07-31
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
Massachusetts Institute of Technology
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139

  Publications

Alberty, Robert A (2008) Rapid-equilibrium rate equations for the enzymatic catalysis of A+B=P+Q over a range of pH. Biophys Chem 132:114-26
Alberty, Robert A (2007) Thermodynamic properties of enzyme-catalyzed reactions involving cytosine, uracil, thymine, and their nucleosides and nucleotides. Biophys Chem 127:91-6
Alberty, Robert A (2007) Changes in binding of hydrogen ions in enzyme-catalyzed reactions. Biophys Chem 125:328-33
Alberty, Robert A (2006) Thermodynamic properties of weak acids involved in enzyme-catalyzed reactions. J Phys Chem B 110:5012-6
Alberty, Robert A (2006) Calculation of equilibrium compositions of systems of enzyme-catalyzed reactions. J Phys Chem B 110:24775-9
Alberty, Robert A (2006) Thermodynamics and kinetics of the glyoxylate cycle. Biochemistry 45:15838-43
Alberty, Robert A (2005) Thermodynamics of the mechanism of the nitrogenase reaction. Biophys Chem 114:115-20
Alberty, Robert A (2005) Calculation of thermodynamic properties of species of biochemical reactants using the inverse Legendre transform. J Phys Chem B 109:9132-9
Alberty, Robert A (2005) Thermodynamic properties of oxidoreductase, transferase, hydrolase, and ligase reactions. Arch Biochem Biophys 435:363-8
Alberty, Robert A (2005) Components and coupling in enzyme-catalyzed reactions. J Phys Chem B 109:2021-6

Showing the most recent 10 out of 28 publications