Mapping the Potential Energy Landscape of Intrinsically Disordered Proteins at Amino Acid Resolution-Reference-Cited by-同舟云学术

Mapping the Potential Energy Landscape of Intrinsically Disordered Proteins at Amino Acid Resolution

Published:2012-08-28 Issue:36 Volume:134 Page:15138-15148
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ozenne Valéry¹,Schneider Robert¹,Yao Mingxi¹,Huang Jie-rong¹,Salmon Loïc¹,Zweckstetter Markus²,Jensen Malene Ringkjøbing¹,Blackledge Martin¹

Affiliation:

1. CEA, CNRS, and UJF-Grenoble 1, Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, 41 Rue Jules Horowitz, Grenoble 38027, France

2. Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, and German Center for Neurodegenerative Diseases (DZNE), 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/ja306905s

Reference57 articles.

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

2. Intrinsic Disorder and Protein Function

3. Unstructural biology coming of age

4. Unfolded Proteins and Protein Folding Studied by NMR

5. Intrinsically unstructured proteins and their functions

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