Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
AUTOR(ES)
Cheung, Margaret S.
FONTE
The National Academy of Sciences
RESUMO
The interplay between structure-search of the native structure and desolvation in protein folding has been explored using a minimalist model. These results support a folding mechanism where most of the structural formation of the protein is achieved before water is expelled from the hydrophobic core. This view integrates water expulsion effects into the funnel energy landscape theory of protein folding. Comparisons to experimental results are shown for the SH3 protein. After the folding transition, a near-native intermediate with partially solvated hydrophobic core is found. This transition is followed by a final step that cooperatively squeezes out water molecules from the partially hydrated protein core.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=117366Documentos Relacionados
- Ultrafast dynamics of solvation: the story so far
- Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation
- How fast is protein hydrophobic collapse?
- Protein model structure evaluation using the solvation free energy of folding.
- Solvation in protein folding analysis: Combination of theoretical and experimental approaches
