Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model
β Scribed by Wei Wang; Peter A Kollman
- Book ID
- 117979578
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 291 KB
- Volume
- 303
- Category
- Article
- ISSN
- 0022-2836
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π SIMILAR VOLUMES
A new method for calculating the total conformational free energy of proteins in water solvent is presented. The method consists of a relatively brief simulation by molecular dynamics with explicit solvent (ES) molecules to produce a set of microstates of the macroscopic conformation. Conformational
A new microscopic model for the quantitative interpretation of solvent effects on molecular eiectrooic spectxa is proposed. The interaction ener& is caicuIated between the solute molecule and a camplet. shell of surrounding solvent nolecutes. The equilibrium configuration is obtained by a procedur
## Abstract SL1 is a stemβloop RNA sequence from the genome of HIVβ1 thought to be the initiation site for the dimerization of the retroviral genomic RNA. The aim of this study is to check the stability in solution of different experimental dimeric structures available in the literature. Two kinds