Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase.
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Solvation Structure and Thermodynamic Mapping (SSTMap): An Open-Source, Flexible Package for the Analysis of Water in Molecular Dynamics Trajectories.Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.Molecular mechanism of substrate selectivity of the arginine-agmatine Antiporter AdiCIn Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function
P2860
Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase.
description
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name
Water-Restructuring Mutations ...... g to Human Carbonic Anhydrase.
@en
Water-Restructuring Mutations ...... g to Human Carbonic Anhydrase.
@nl
type
label
Water-Restructuring Mutations ...... g to Human Carbonic Anhydrase.
@en
Water-Restructuring Mutations ...... g to Human Carbonic Anhydrase.
@nl
prefLabel
Water-Restructuring Mutations ...... g to Human Carbonic Anhydrase.
@en
Water-Restructuring Mutations ...... g to Human Carbonic Anhydrase.
@nl
P2093
P2860
P356
P1476
Water-Restructuring Mutations ...... ng to Human Carbonic Anhydrase
@en
P2093
Banumathi Sankaran
George M Whitesides
Kyungtae Kang
Madhavi Sastry
Peter H Zwart
Woody Sherman
P2860
P304
P356
10.1002/ANIE.201609409
P407
P50
P577
2017-03-02T00:00:00Z