Molecular dynamics study of the stability of staphylococcal nuclease mutants: component analysis of the free energy difference of denaturation
- 1 April 1993
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1163 (1) , 81-88
- https://doi.org/10.1016/0167-4838(93)90282-v
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Simulation analysis of the stability mutant R96H of T4 lysozymeBiochemistry, 1991
- Contributions of the large hydrophobic amino acids to the stability of staphylococcal nucleaseBiochemistry, 1990
- Free energy calculations on protein stability: Thr-157 .fwdarw. Val-157 mutation of T4 lysozymeJournal of the American Chemical Society, 1989
- The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+ and the inhibitor pdTp, refined at 1.65 ÅProteins-Structure Function and Bioinformatics, 1989
- Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reactionBiochemistry, 1988
- Free Energy Calculations by Computer SimulationScience, 1987
- Dynamics and design of enzymes and inhibitorsJournal of the American Chemical Society, 1986
- Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturationProteins-Structure Function and Bioinformatics, 1986
- The problem of the stability of globular proteinsMolecular and Cellular Biochemistry, 1981
- The Stability of Globular ProteinCRC Critical Reviews in Biochemistry, 1975