Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected (13)C CPMG relaxation dispersion

Protein dynamics on the millisecond time scale commonly reflect conformational transitions between distinct functional states. NMR relaxation dispersion experiments have provided important insights into biologically relevant dynamics with site-specific resolution, primarily targeting the protein bac...

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Detalles Bibliográficos
Autores principales: Weininger, Ulrich, Respondek, Michal, Akke, Mikael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2012
Materias:
Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427480/
https://www.ncbi.nlm.nih.gov/pubmed/22833056
http://dx.doi.org/10.1007/s10858-012-9656-z

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427480/
https://www.ncbi.nlm.nih.gov/pubmed/22833056
http://dx.doi.org/10.1007/s10858-012-9656-z

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