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Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites

Cryptic allosteric sites—transient pockets in a folded protein that are invisible to conventional experiments but can alter enzymatic activity via allosteric communication with the active site—are a promising opportunity for facilitating drug design by greatly expanding the repertoire of available d...

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Detalhes bibliográficos
Main Authors: Bowman, Gregory R., Geissler, Phillip L.
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2012
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3406870/
https://ncbi.nlm.nih.gov/pubmed/22753506
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1209309109
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