Cargando…
Protein conformational entropy is not slaved to water
Conformational entropy can be an important element of the thermodynamics of protein functions such as the binding of ligands. The observed role for conformational entropy in modulating molecular recognition by proteins is in opposition to an often-invoked theory for the interaction of protein molecu...
Autores principales: | Marques, Bryan S., Stetz, Matthew A., Jorge, Christine, Valentine, Kathleen G., Wand, A. Joshua, Nucci, Nathaniel V. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7567893/ https://www.ncbi.nlm.nih.gov/pubmed/33067552 http://dx.doi.org/10.1038/s41598-020-74382-5 |
Ejemplares similares
-
Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy
por: O'Brien, Evan S., et al.
Publicado: (2020) -
Pressure, motion, and conformational entropy in molecular recognition by proteins
por: Caro, José A., et al.
Publicado: (2022) -
The role of conformational entropy in molecular recognition by calmodulin
por: Marlow, Michael S., et al.
Publicado: (2010) -
Reconciling Mediating and Slaving Roles of Water in Protein Conformational Dynamics
por: Zhao, Li, et al.
Publicado: (2013) -
Reverse
Micelles As a Platform for Dynamic Nuclear
Polarization in Solution NMR of Proteins
por: Valentine, Kathleen G., et al.
Publicado: (2014)