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The Thermodynamic Influence of Trapped Water Molecules on a Protein–Ligand Interaction
Author(s) -
Stegmann Christian M.,
Seeliger Daniel,
Sheldrick George M.,
de Groot Bert L.,
Wahl Markus C.
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.200900481
Subject(s) - molecule , chemistry , ligand (biochemistry) , resolution (logic) , crystallography , calorimetry , chemical physics , cyclophilin , molecular dynamics , thermodynamics , computational chemistry , biochemistry , physics , organic chemistry , receptor , gene , artificial intelligence , computer science
Water molecules doing time : Atomic‐resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein–ligand interaction.