Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets. 1. NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the Peptide Sos-Reference-Cited by-同舟云学术

Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets. 1. NMR and MD Characterization of the Complex between the c-Crk N-SH3 Domain and the Peptide Sos

Published:2014-10-07 Issue:41 Volume:53 Page:6473-6495
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Xue Yi¹,Yuwen Tairan¹,Zhu Fangqiang²,Skrynnikov Nikolai R.¹³

Affiliation:

1. Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, United States

2. Department of Physics, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202, United States

3. Laboratory of Biomolecular NMR, St. Petersburg State University, St. Petersburg 199034, Russia

Funder

Division of Molecular and Cellular Biosciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi500904f

Reference162 articles.

1. The Conformational Mobility of Proteins and its Functional Significance

2. Why are ?natively unfolded? proteins unstructured under physiologic conditions?

3. Sequence complexity of disordered protein

4. Comparing and Combining Predictors of Mostly Disordered Proteins

5. Controlled Chaos

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