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Serge N. Timasheff

Serge N. Timasheff

D-Index & Metrics

Chemistry

D-Index
84
Citations
35346
World Ranking
2757
National Ranking
950

Research.com Recognitions

  • 1989 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 1972 - Fellow of John Simon Guggenheim Memorial Foundation

Overview

Serge N. Timasheff was affiliated with Brandeis University in the United States. Their research work focused primarily on materials science, with a specialization in materials chemistry. The main topics of their scientific contributions included crystallization and solubility studies as well as X-ray diffraction in crystallography.

Their publication record featured papers published in The Cambridge Structural Database, which was their frequent publication venue. Notable papers released in 2021 included:

  • CCDC 2064587: Experimental Crystal Structure Determination (2021, The Cambridge Structural Database)
  • CCDC 2064586: Experimental Crystal Structure Determination (2021, The Cambridge Structural Database)

Collaborations played a significant role in their work. Frequent co-authors included Miriam Rossi, Marina J. Gorbunoff, Francesco Caruso, Bernadette Wing, and Bernardo Pérez-Ramírez. Each of these collaborators co-authored multiple publications with Timasheff, contributing to the development of research in crystallography and materials chemistry.

Timasheff's scientific efforts centered on advancing understanding of crystallization phenomena and the application of X-ray diffraction techniques to analyze crystal structures. Their research contributed to the detailed exploration of solubility behaviors and structural determination of materials, providing data essential for the materials science community.

In recognition of their scientific contributions, Timasheff was awarded Fellowships by notable organizations. They became a Fellow of the American Association for the Advancement of Science (AAAS) in 1989 and earlier received a Fellowship at the John Simon Guggenheim Memorial Foundation in 1972.

Best Publications

  • Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures

    Kunihiko Gekko;Serge N. Timasheff

  • The stabilization of proteins by sucrose.

    James Lee;S. N. Timasheff

  • The control of protein stability and association by weak interactions with water: how do solvents affect these processes?

    Serge N. Timasheff

  • Stabilization of protein structure by sugars.

    Tsutomu Arakawa;Serge N. Timasheff

  • The stabilization of proteins by osmolytes.

    T. Arakawa;S.N. Timasheff

  • Preferential interactions of proteins with salts in concentrated solutions

    Tsutomu Arakawa;Serge N. Timasheff

  • Structure and stability of biological macromolecules

    Serge N. Timasheff;Gerald D. Fasman

  • Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding.

    Tsutomu Arakawa;Serge N. Timasheff

  • Protein hydration, thermodynamic binding, and preferential hydration.

    Serge N Timasheff

  • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components

    Unknown

  • Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects.

    Tsutomu Arakawa;Daisuke Ejima;Kouhei Tsumoto;Noriyuki Obeyama

  • Thermodynamic and kinetic examination of protein stabilization by glycerol

    Kunihiko Gekko;Serge N. Timasheff

  • Mechanism of poly(ethylene glycol) interaction with proteins.

    Tsutomu Arakawa;Serge N. Timasheff

  • Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated.

    Unknown

  • The thermodynamic mechanism of protein stabilization by trehalose.

    Guifu Xie;Serge N. Timasheff

  • Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein.

    Tiao-Yin Lin;Serge N. Timasheff

  • Preferential interactions of proteins with solvent components in aqueous amino acid solutions

    Tsutomu Arakawa;Serge N. Timasheff

  • Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols.

    Rajiv Bhat;Serge N. Timasheff

  • Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride.

    James C. Lee;Serge N. Timasheff

  • Theory of protein solubility.

    Tsutomu Arakawa;Serge N. Timasheff

  • In vitro reconstitution of calf brain microtubules: effects of solution variables.

    James C. Lee;James C. Lee;Serge N. Timasheff

  • Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.

    Serge N. Timasheff

Frequent Co-Authors

José Manuel Andreu
José Manuel Andreu Spanish National Research Council
James Lee
James Lee The Francis Crick Institute
John G. Kirkwood
John G. Kirkwood Yale University
Giorgio Bernardi
Giorgio Bernardi University of Rome Tor Vergata
Julian M. Sturtevant
Julian M. Sturtevant Yale University
Kouhei Tsumoto
Kouhei Tsumoto University of Tokyo
Lizbeth Hedstrom
Lizbeth Hedstrom Brandeis University
Robert Seckler
Robert Seckler University of Potsdam
Yoshikazu Tanaka
Yoshikazu Tanaka Tohoku University
Robert H. Abeles
Robert H. Abeles Brandeis University

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