Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutantsElectronic supplementary information (ESI) available: Fig. S1: regions of NOESY spectra with cross-peaks providing NOEs restraining asparagine N51 in the NMR structure; Fig. S2: typical snapshot from the restrained MD simulation of the K52E mutant of the Drosophila EnHD in the g+ conformation along the torsion angle N-CA-CB-CG of asparagine N51; Fig. S3: NOESY spectra taken a

Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutantsElectronic supplementary information (ESI) available: Fig. S1: regions of NOESY spectra with cross-peaks providing NOEs restraining asparagine N51 in the NMR structure; Fig. S2: typical snapshot from the restrained MD simulation of the K52E mutant of the Drosophila EnHD in the g+ conformation along the torsion angle N-CA-CB-CG of asparagine N51; Fig. S3: NOESY spectra taken a

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-H π hydrogen bonding and lone-pair π interactions wa...

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Hauptverfasser: Špa ková, Nad'a, Trošanová, Zuzana, Šebesta, Filip, Jansen, Séverine, Burda, Jaroslav V, Srb, Pavel, Zachrdla, Milan, ídek, Lukáš, Kozelka, Ji í
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