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Mobility-based prediction of hydration structures of protein surfaces
2015
Bioinformatics
Motivation: Hydration largely determines solubility, aggregation of proteins and influences interactions between proteins and drug molecules. Despite the importance of hydration, structural determination of hydration structure of protein surfaces is still challenging from both experimental and theoretical viewpoints. The precision of experimental measurements is often affected by fluctuations and mobility of water molecules resulting in uncertain assignment of water positions. Results: Our
doi:10.1093/bioinformatics/btv093
pmid:25682067
fatcat:jl5vutvoq5dedaux4f574dw4rq