pH Dependence of binding reactions from free energy simulations and macroscopic continuum electrostatic calculations: Application to 2′GMP/3′GMP binding to ribonuclease T1 and implications for catalysis
- 7 April 1995
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 247 (4) , 774-807
- https://doi.org/10.1016/s0022-2836(05)80155-x
Abstract
No abstract availableKeywords
This publication has 84 references indexed in Scilit:
- Molecular recognition in proteinsJournal of Molecular Biology, 1994
- Hidden Thermodynamics of Mutant Proteins: A Molecular Dynamics AnalysisScience, 1989
- Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparisonProteins-Structure Function and Bioinformatics, 1988
- Electrostatic effects and hydrogen exchange behaviour in proteinsJournal of Molecular Biology, 1987
- Modification of glu 58, an amino acid of the active center of ribonuclease T1, to Gln and AspBiochemical and Biophysical Research Communications, 1986
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Calculation of the electric potential in the active site cleft due to α-helix dipolesJournal of Molecular Biology, 1982
- Spectrophotometric titration of a single carboxyl group at the active site of ribonuclease T1Biochemistry, 1977
- A mathematical model for structure-function relations in hemoglobinJournal of Molecular Biology, 1972