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- W2015415511 abstract "Using the IGg binding domain of protein L from Streptoccocal magnus (ProtL) as a case study, we investigated how the anions of the Hofmeister series affect protein stability. To that end, a suite of lysine-to-glutamine modifications were obtained and structurally and thermodynamically characterized. The changes in stability introduced with the mutation are related to the solvent-accessible area of the side chain, specifically to the solvation of the nonpolar moiety of the residue. The thermostability for the set of ProtL mutants was determined in the presence of varying concentrations (0-1 M) of six sodium salts from the Hofmeister series: sulfate, phosphate, fluoride, nitrate, perchlorate, and thiocyanate. For kosmotropic anions (sulfate, phosphate, and fluoride), the stability changes induced by the cosolute (encoded in m(3)=deltaDeltaG(0)/deltaC(3)) are proportional to the surface changes introduced with the mutation. In contrast, the m(3) values measured for chaotropic anions are much more independent of such surface modifications. Our results are consistent with a model in which the increase in the solution surface tension induced by the anion stabilizes the folded conformation of the protein. This contribution complements the nonspecific and weak interactions between the ions and the protein backbone that shift the equilibrium toward the unfolded state." @default.
- W2015415511 created "2016-06-24" @default.
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- W2015415511 creator A5032192901 @default.
- W2015415511 creator A5043950168 @default.
- W2015415511 creator A5054255043 @default.
- W2015415511 date "2009-11-01" @default.
- W2015415511 modified "2023-10-17" @default.
- W2015415511 title "Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation" @default.
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- W2015415511 doi "https://doi.org/10.1016/j.bpj.2009.08.029" @default.
- W2015415511 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2770621" @default.
- W2015415511 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19883603" @default.
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