Escher: A new docking procedure applied to the reconstruction of protein tertiary structure

Escher: A new docking procedure applied to the reconstruction of protein tertiary structure Evaluation of Surface Complementarity, Hydrogen bonding, and Electrostatic interaction in molecular Recognition (ESCHER) is a new docking procedure consisting of three modules that work in series. The first module evaluates the geometric complementarity and produces a set of rough solutions for the docking problem. The second module identifies molecular collisions within those solutions, and the third evaluates their electrostatic complementarity. We describe the algorithm and its application to the docking of cocrystallized protein domains and unbound components of protein‐protein complexes. Furthermore, ESCHER has been applied to the reassociation of secondary and supersecondary structure elements. The possibility of applying a docking method to the problem of protein structure prediction is discussed. Proteins 28:556–567, 1997. © 1997 Wiley‐Liss, Inc. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Proteins: Structure Function and Bioinformatics Wiley

Escher: A new docking procedure applied to the reconstruction of protein tertiary structure

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Publisher
Wiley
Copyright
Copyright © 1997 Wiley‐Liss, Inc.
ISSN
0887-3585
eISSN
1097-0134
DOI
10.1002/(SICI)1097-0134(199708)28:4<556::AID-PROT9>3.3.CO;2-C
Publisher site
See Article on Publisher Site

Abstract

Evaluation of Surface Complementarity, Hydrogen bonding, and Electrostatic interaction in molecular Recognition (ESCHER) is a new docking procedure consisting of three modules that work in series. The first module evaluates the geometric complementarity and produces a set of rough solutions for the docking problem. The second module identifies molecular collisions within those solutions, and the third evaluates their electrostatic complementarity. We describe the algorithm and its application to the docking of cocrystallized protein domains and unbound components of protein‐protein complexes. Furthermore, ESCHER has been applied to the reassociation of secondary and supersecondary structure elements. The possibility of applying a docking method to the problem of protein structure prediction is discussed. Proteins 28:556–567, 1997. © 1997 Wiley‐Liss, Inc.

Journal

Proteins: Structure Function and BioinformaticsWiley

Published: Aug 1, 1997

Keywords: molecular recognition; automated docking; protein domains; secondary structure elements

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