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Serge N. Timasheff
Researcher at Brandeis University
Publications - 8
Citations - 1544
Serge N. Timasheff is an academic researcher from Brandeis University. The author has contributed to research in topics: Binding constant & Microtubule. The author has an hindex of 7, co-authored 8 publications receiving 1468 citations. Previous affiliations of Serge N. Timasheff include Spanish National Research Council.
Papers
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Journal ArticleDOI
Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components.
TL;DR: It is shown that the measured change of the amount of water in contact with protein during the course of the reaction modulated by an osmolyte is a change in preferential hydration that is strictly a measure of the cosolvent chemical potential perturbation by the protein in the ternary water–protein–cosolvent system.
Book ChapterDOI
Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated
Journal ArticleDOI
Preferential interactions of urea with lysozyme and their linkage to protein denaturation.
Serge N. Timasheff,Guifu Xie +1 more
TL;DR: Both the stabilization and destabilization of proteins by co-solvents are controlled predominantly by preferential interactions with peptide groups newly exposed on denaturation.
Journal ArticleDOI
Role of the colchicine ring a and its methoxy groups in the binding to tubulin and microtubule inhibition
José Manuel Andreu,Bernardo Perez-Ramirez,Marina J. Gorbunoff,David Ayala,Serge N. Timasheff +4 more
TL;DR: It is concluded that ring A of COL is not germane to the mechanism of the inhibition of tubulin self-assembly, and serves only as a complex-stabilizing anchor.
Journal ArticleDOI
Thermodynamic binding and site occupancy in the light of the Schellman exchange concept.
TL;DR: An analysis of Schellman's treatment of preferential interactions is presented, as viewed by a laboratory practitioner of the art, which demonstrates the effect of site heterogeneity on the ligand concentration dependencies of site occupancy, preferential binding and the thermodynamic quantities, enthalpy, entropy and Gibbs free energy.