ArticleBiophysical journal2012
Quantitative characterization of local protein solvation to predict solvent effects on protein structure.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 0 citations in OpenAlex.
- Interplay of protein fluctuation and associated water dynamics in osmolyte-induced stabilization.Biophysical journal · 2025Article
- Solvent accessible surface area-assessed molecular basis of osmolyte-induced protein stability.RSC advances · 2024Article
- Rapid isolation and quantification of extracellular vesicles from suspension-adapted human embryonic kidney cells using capillary-channeled polymer fiber spin-down tips.Electrophoresis · 2023Article
- Computing the Structural Dynamics of RVFV L Protein Domain in Aqueous Glycerol Solutions.Biomolecules · 2021Article
- Characterizing Hydropathy of Amino Acid Side Chain in a Protein Environment by Investigating the Structural Changes of Water Molecules Network.Frontiers in molecular biosciences · 2021Article
- Polarizable empirical force field for acyclic polyalcohols based on the classical Drude oscillator.Biopolymers · 2013Article
- Quantifying the molecular origins of opposite solvent effects on protein-protein interactions.PLoS computational biology · 2013Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Characterization of solvent preferences of proteins is essential to the understanding of solvent effects on protein structure and stability. Although it is generally believed that solvent preferences at distinct loci of a protein surface may differ, quantitative characterization of local protein solvation has remained elusive. In this study, we show that local solvation preferences can be quantified over the entire protein surface from extended molecular dynamics simulations. By subjecting microsecond trajectories of two proteins (lysozyme and antibody fragment D1.3) in 4 M glycerol to rigorous statistical analyses, solvent preferences of individual protein residues are quantified by local preferential interaction coefficients. Local solvent preferences for glycerol vary widely from residue to residue and may change as a result of protein side-chain motions that are slower than the longest intrinsic solvation timescale of ∼10 ns. Differences of local solvent preferences between distinct protein side-chain conformations predict solvent effects on local protein structure in good agreement with experiment. This study extends the application scope of preferential interaction theory and enables molecular understanding of solvent effects on protein structure through comprehensive characterization of local protein solvation.
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