Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets: 2. The Model of Encounter Complex Involving the Double Mutant of the c-Crk N-SH3 Domain and 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: 2. The Model of Encounter Complex Involving the Double Mutant of the c-Crk N-SH3 Domain and Peptide Sos

Published:2016-03-14 Issue:12 Volume:55 Page:1784-1800
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Yuwen Tairan¹,Xue Yi¹,Skrynnikov Nikolai R.¹²

Affiliation:

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

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

Funder

Division of Molecular and Cellular Biosciences

Russian Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b01283

Reference72 articles.

1. Structure and Dynamics of the Aβ21–30 Peptide from the Interplay of NMR Experiments and Molecular Simulations

2. Atomic-Level Characterization of the Ensemble of the Aβ(1–42) Monomer in Water Using Unbiased Molecular Dynamics Simulations and Spectral Algorithms

3. Molecular Mechanisms of Ion-Specific Effects on Proteins

4. A Preformed Binding Interface in the Unbound Ensemble of an Intrinsically Disordered Protein: Evidence from Molecular Simulations

5. A Relationship between the Transient Structure in the Monomeric State and the Aggregation Propensities of α-Synuclein and β-Synuclein

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