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Evidence for CCl/CBr⋅⋅⋅π Interactions as an Important Contribution to Protein–Ligand Binding Affinity
Author(s) -
Matter Hans,
Nazaré Marc,
Güssregen Stefan,
Will David W.,
Schreuder Herman,
Bauer Armin,
Urmann Matthias,
Ritter Kurt,
Wagner Michael,
Wehner Volkmar
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200806219
Subject(s) - chemistry , bromine , non covalent interactions , chlorine , generality , ligand (biochemistry) , stereochemistry , crystallography , computational chemistry , molecule , hydrogen bond , biochemistry , organic chemistry , psychology , receptor , psychotherapist
Attractive chlorine : Noncovalent interactions between chlorine or bromine atoms and aromatic rings in proteins open up a new method for the manipulation of molecular recognition. Substitution at distinct positions of two factor Xa inhibitors improves the free energy of binding by interaction with a tyrosine unit. The generality of this motif was underscored by multiple crystal structures as well as high‐level quantum chemical calculations (see picture).