Article
Contribution of the hydrophobic effect to protein stability: analysis based on simulations of the Ile-96----Ala mutation in barnase.
Proceedings of the National Academy of Sciences of the United States of America - 1 Dec 1991
Prevost M, Wodak S J, Tidor B, Karplus M
Abstract excerpt
Molecular dynamics simulations have been used to compute the difference in the unfolding free energy between wild-type barnase and the mutant in which Ile-96 is replaced by alanine. The simulations yield results (-3.42 and -5.21 kcal/mol) that compare favorably with experimental values (-3.3 and -4.0 kcal/mol). The major contributions to the free energy difference arise from bonding terms involving degrees of...
Topics
- Alanine
- Amino Acid Sequence
- Bacillus
- Bacterial Proteins
- Calorimetry
- Computer Simulation
- Drug Stability
- Enzyme Stability
- Isoleucine
- Models, Molecular
- Mutation