Article
Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants.
Physical chemistry chemical physics : PCCP - 9 May 2018
Špačková Nad'a, Trošanová Zuzana, Šebesta Filip, Jansen Séverine, Burda Jaroslav V, Srb Pavel, Zachrdla Milan, Žídek Lukáš, Kozelka Jiří
Abstract excerpt
Water molecules can interact with aromatic moieties using either their O-H bonds or their lone-pairs of electrons. In proteins, water-π interactions have been reported to occur with tryptophan and histidine residues, and dynamic exchange between O-Hπ hydrogen bonding and lone-pairπ interactions was suggested to take place, based on ab initio calculations. Here we used classical and QM/MM molecular dynamics...
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