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Ward, L D; Seckler, R; Timasheff, S N (1994) Energy transfer studies of the distances between the colchicine, ruthenium red, and bisANS binding sites on calf brain tubulin. Biochemistry 33:11900-8
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Kita, Y; Arakawa, T; Lin, T Y et al. (1994) Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry 33:15178-89
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Perez-Ramirez, B; Timasheff, S N (1994) Cosolvent modulation of the tubulin-colchicine GTPase-activating conformational change: strength of the enzymatic activity. Biochemistry 33:6262-7
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Perez-Ramirez, B; Shearwin, K E; Timasheff, S N (1994) The colchicine-induced GTPase activity of tubulin: state of the product. Activation by microtubule-promoting cosolvents. Biochemistry 33:6253-61
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Shearwin, K E; Perez-Ramirez, B; Timasheff, S N (1994) Linkages between the dissociation of alpha beta tubulin into subunits and ligand binding: the ground state of tubulin is the GDP conformation. Biochemistry 33:885-93
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Ward, L D; Timasheff, S N (1994) Cooperative multiple binding of bisANS and daunomycin to tubulin. Biochemistry 33:11891-9
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Shearwin, K E; Timasheff, S N (1994) Effect of colchicine analogues on the dissociation of alpha beta tubulin into subunits: the locus of colchicine binding. Biochemistry 33:894-901
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Lin, T Y; Timasheff, S N (1994) Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. Biochemistry 33:12695-701
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Bhat, R; Timasheff, S N (1992) Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Sci 1:1133-43
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Prakash, V; Timasheff, S N (1992) Aging of tubulin at neutral pH: the destabilizing effect of vinca alkaloids. Arch Biochem Biophys 295:137-45
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Showing the most recent 10 out of 47 publications
