Modeling Side-chain Conformation for Homologous Proteins Using an Energy-based Rotamer Search
β Scribed by Charles Wilson; Lydia M. Gregoret; David A. Agard
- Book ID
- 115625869
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 713 KB
- Volume
- 229
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
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
## Abstract The hydration free energies of amino acid side chains are an important determinant of processes that involve partitioning between different environments, including protein folding, protein complex formation, and proteinβmembrane interactions. Several recent papers have shown that calcul