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Site-specific hydration dynamics of globular proteins and the role of constrained water in solvent exchange with amphiphilic cosolvents

The thermodynamic driving forces for protein folding, association and function are often determined by protein-water interactions. With a novel covalently bound labeling approach, we have used sensitive vibrational probes, site-selectively conjugated to two lysozyme variants–in conjunction with ultr...

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Detalhes bibliográficos
Main Authors: King, John T., Arthur, Evan J., Brooks, Charles L., Kubarych, Kevin J.
Formato: Artigo
Idioma:Inglês
Publicado em: 2012
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3422398/
https://ncbi.nlm.nih.gov/pubmed/22530969
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jp300835k
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