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Direct Investigation of Slow Correlated Dynamics in Proteins via Dipolar Interactions

The synchronization of native state motions as they transition between microstates influences catalysis kinetics, mediates allosteric interactions and reduces the conformational entropy of proteins. However, it has proven difficult to describe native microstates because they are usually minimally fr...

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Detalhes bibliográficos
Publicado no:J Am Chem Soc
Main Authors: Fenwick, R. Bryn, Schwieters, Charles D., Vögeli, Beat
Formato: Artigo
Idioma:Inglês
Publicado em: 2016
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC5055379/
https://ncbi.nlm.nih.gov/pubmed/27331619
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.6b01447
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