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• W2005509806 endingPage "5267" @default.
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• W2005509806 abstract "Atomistic molecular dynamics simulations are used to probe changes in the nature and subnanosecond dynamical behavior of solvation waters that accompany partial denaturation of the globular protein, human alpha-lactalbumin. A simulated ensemble of subcompact conformers, similar to the molten globule state of human alpha-lactalbumin, demonstrates a marginal increase in the amount of surface solvation relative to the native state. This increase is accompanied by subtle but distinct enhancement in surface water dynamics, less favorable protein-water interactions, and a marginal decrease in the anomalous behavior of solvation water dynamics. The extent of solvent influx is not proportional to the increased surface area, and the partially denatured conformers are less uniformly solvated compared to their native counterpart. The observed solvation in partially denatured conformers is lesser in extent compared to earlier experimental estimates in molten globule states, and is consistent with more recent descriptions based on nuclear magnetic relaxation dispersion studies." @default.
• W2005509806 created "2016-06-24" @default.
• W2005509806 creator A5023659460 @default.
• W2005509806 creator A5054892499 @default.
• W2005509806 creator A5058734762 @default.
• W2005509806 date "2008-12-01" @default.
• W2005509806 modified "2023-09-30" @default.
• W2005509806 title "Hydration Dynamics in a Partially Denatured Ensemble of the Globular Protein Human α-Lactalbumin Investigated with Molecular Dynamics Simulations" @default.
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• W2005509806 doi "https://doi.org/10.1529/biophysj.108.136531" @default.
• W2005509806 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2586557" @default.
• W2005509806 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18775960" @default.
• W2005509806 hasPublicationYear "2008" @default.
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