NMR Characterization of Long-Range Order in Intrinsically Disordered Proteins-Reference-Cited by-同舟云学术

NMR Characterization of Long-Range Order in Intrinsically Disordered Proteins

Published:2010-05-25 Issue:24 Volume:132 Page:8407-8418
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Salmon Loïc¹,Nodet Gabrielle¹,Ozenne Valéry¹,Yin Guowei¹,Jensen Malene Ringkjøbing¹,Zweckstetter Markus¹,Blackledge Martin¹

Affiliation:

1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; CNRS; UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, France, and NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja101645g

Reference69 articles.

1. Natively unfolded proteins: A point where biology waits for physics

2. Intrinsic Disorder and Protein Function

3. Intrinsically unstructured proteins

4. Coupling of folding and binding for unstructured proteins

5. Atomic-level characterization of disordered protein ensembles

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