A carregar...
The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions.
Protein-solvent interactions were analyzed using an optimization parameter based on the ratio of the solvent-accessible area in the native and the unfolded protein structure. The calculations were performed for a set of 183 nonhomologous proteins with known three-dimensional structure available in t...
Na minha lista:
| Main Authors: | , , |
|---|---|
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Cold Spring Harbor Laboratory Press
1995
|
| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143201/ https://ncbi.nlm.nih.gov/pubmed/8520477 |
| Tags: |
Adicionar Tag
Sem tags, seja o primeiro a adicionar uma tag!
|