article Open AccessTop 10% cited
How Hofmeister ion interactions affect protein stability
Biophysical Journal · 1996 · Vol. 71(4) · pp. 2056–2063
Robert L. Baldwin✉(Stanford University)
Spectroscopy and Quantum Chemical StudiesMass Spectrometry Techniques and ApplicationsProtein Structure and DynamicsHofmeister seriesChemistryIonSalt (chemistry)Chemical physicsIonic strengthSalting outComputational chemistryIonic bondingCrystallography
MeSH terms
Drug StabilityKineticsModels, ChemicalOsmolar ConcentrationPeptidesProtein ConformationProteinsSolutionsSurface TensionThermodynamicsProtein Structure, Secondary
Citations
1,127
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8.28
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32
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References
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl .alpha.-chymotrypsin using different denaturants
Biochemistry · 1988 · 1,585 citations
Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
Archives of Biochemistry and Biophysics · 1977 · 913 citations
Proteins, amino acids and peptides
Journal of the Franklin Institute · 1943 · 2,172 citations
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