Application of hydration thermodynamics to the evaluation of protein structures and protein-ligand binding

DOI10.3390/E14081443zbMATH Open1323.92148OpenAlexW2055594020MaRDI QIDQ406154FDOQ406154

Authors: Yuichi Harano 

Publication date: 8 September 2014

Published in: Entropy (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.3390/e14081443

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zbMATH Keywords

binding free energyhydration entropyhydration thermodynamicsprotein structure stability

Mathematics Subject Classification ID

Protein sequences, DNA sequences (92D20) Classical and relativistic thermodynamics (80A10)

Cites Work

• Analysis of the bulk and surface-induced structure of electrolyte solutions using intergral equation theories
• Theory of Classical Fluids: Hyper-Netted Chain Approximation. III
• Introduction to special issue on water and associated liquids

Cited In (9)

• Quantitative prediction of the thermal motion and intrinsic disorder of protein cofactors in crystalline state: a case study on halide anions
• Implication of crystal water molecules in inhibitor binding at ALR2 active site
• An outlook on biothermodynamics: Needs, problems, and new developments. I. Stability and hydration of proteins
• Ultrametric theory of conformational dynamics of protein molecules in a functional state and the description of experiments on the kinetics of CO binding to myoglobin
• Title not available (Why is that?)
• The equivalent potential of water molecules for electronic structure of lysine
• Energy landscapes of protein self-assembly: lessons from native topology-based models
• Scoring functions for protein-RNA complex structure prediction: advances, applications, and future directions
• Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymes

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