Docking of Protein−Protein Complexes on the Basis of Highly Ambiguous Intermolecular Distance Restraints Derived from 1HN/15N Chemical Shift Mapping and Backbone 15N−1H Residual Dipolar Couplings Using Conjoined Rigid Body/Torsion Angle Dynamics-Reference-Cited by-同舟云学术

Docking of Protein−Protein Complexes on the Basis of Highly Ambiguous Intermolecular Distance Restraints Derived from 1HN/15N Chemical Shift Mapping and Backbone 15N−1H Residual Dipolar Couplings Using Conjoined Rigid Body/Torsion Angle Dynamics

Published:2003-02-15 Issue:10 Volume:125 Page:2902-2912
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Clore G. Marius¹,Schwieters Charles D.¹

Affiliation:

1. Contribution from the Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0510, and Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja028893d

Reference55 articles.

1. TreeDock: A Tool for Protein Docking Based on Minimizing van der Waals Energies

2. Protein-protein docking with multiple residue conformations and residue substitutions

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