Probing Transient Conformational States of Proteins by Solid-State R(1ρ) Relaxation-Dispersion NMR Spectroscopy**

The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally accessible conformations are connected, and understanding their structures and relative energies is crucial in rationalizing protein function....

Descripción completa

Detalles Bibliográficos
Autores principales: Ma, Peixiang, Haller, Jens D, Zajakala, Jérémy, Macek, Pavel, Sivertsen, Astrid C, Willbold, Dieter, Boisbouvier, Jérôme, Schanda, Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2014
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3997346/
https://www.ncbi.nlm.nih.gov/pubmed/24644028
http://dx.doi.org/10.1002/anie.201311275

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3997346/
https://www.ncbi.nlm.nih.gov/pubmed/24644028
http://dx.doi.org/10.1002/anie.201311275

Ejemplares similares