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Biochemistry|February 20, 1990
Preferential interactions determine protein solubility in three-component solutions: the MgCl2 systemT Arakawa, R Bhat, S N TimasheffBiochemistry|December 20, 1994
Contribution of the surface free energy perturbation to protein-solvent interactionsY Kita, T Arakawa, T Y Lin, et al.Proceedings of the National Academy of Sciences of the United States of America|June 24, 1998
In disperse solution, "osmotic stress" is a restricted case of preferential interactionsS N TimasheffArchives of Biochemistry and Biophysics|May 15, 1992
Aging of tubulin at neutral pH: stabilization by colchicine and its analoguesV Prakash, S N TimasheffAnalytical Biochemistry|May 1, 1983
The resolution of bimodal peaks in the analytical ultracentrifuge in the presence and absence of ligandsV Prakash, S N TimasheffThe Journal of Biological Chemistry|February 10, 1983
The interaction of vincristine with calf brain tubulinV Prakash, S N TimasheffBiochemistry|August 4, 1981
Thermodynamic and kinetic examination of protein stabilization by glycerolK Gekko, S N TimasheffProtein Science : a Publication of the Protein Society|September 1, 1992
Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycolsR Bhat, S N TimasheffArchives of Biochemistry and Biophysics|May 15, 1992
Aging of tubulin at neutral pH: the destabilizing effect of vinca alkaloidsV Prakash, S N TimasheffBiochemistry|September 22, 1987
Inhibition of tubulin self-assembly and tubulin-colchicine GTPase activity by guanosine 5'-(gamma-fluorotriphosphate)O Monasterio, S N TimasheffPageof 54