Info

Tanford, C. (1968). Protein denaturation. Adv. Protein Chem. 23, 121-282.

Tanford, C., Pain, R. H., and Otchin, N. S. (1966). Equilibrium and kinetics of the unfolding of lysozyme (muramidase) by guanidine hydrochloride. J. Mol. Biol. 15, 489-504.

Tirado-Rives, J., Orozco, M., andJorgensen, W. L. (1997). Molecular dynamics simulations of the unfolding of barnase in water and 8 M aqueous urea. Biochemistry 36, 7313-7329.

Tsai, J., Gerstein, M., and Levitt, M. (1996). Keeping the shape but changing the charges: A simulation study of urea and its iso-steric analogs. J. Chem. Phys. 104, 9417-9430.

Turner, J., Finney, J. L., and Soper, A. K. (1991). Neutron diffraction studies of structure in aqueous solutions ofurea and tetramethylammonium chloride and in methanol. Zeitschrift Naturforschung Sect. a J. Phys. Sci. 46, 73-83.

Vishnyakov, A., Widmalm, G., Kowalewski, J., and Laaksonen, A. (1999). Molecular dynamics simulation of the alpha-D-Manp-(1 —> 3)-beta-D-Glcp-OMe disaccharide in water and water DMSO solution. J. Am. Chem. Soc. 121, 5403-5412.

Wernet, P., Nordlund, D., Bergmann, U., Cavalleri, M., Odelius, M., Ogasawara, H., Naslund, L. A., Hirsch, T. K., Ojamae, L., Glatzel, P., Pettersson, L. G. M., and Nilsson, A. (2004). The structure of the first coordination shell in liquid water. Science 304, 995-999.

Whitney, P. L., and Tanford, C. (1965). Recovery of specific activity after complete unfolding and reduction of an antibody fragment. Proc. Natl. Acad. Sci. USA 53, 524-532.

Yamaguchi, T., Benmore, C. J., and Soper, A. K. (2000). The structure of subcritical and supercritical methanol by neutron diffraction, empirical potential structure refinement, and spherical harmonic analysis. J. Chem. Phys. 112, 8976-8987.

Zhang, Z. Y., Zhu, Y. J., and Shi, Y. Y. (2001). Molecular dynamics simulations of urea and thermal-induced denaturation of S-peptide analogue. Biophys. Chem. 89, 145-162.

Zou, Q., Bennion, B. J., Daggett, V., and Murphy, K. P. (2002). The molecular mechanism ofstabilization ofproteins by TMAO and its ability to counteract the effects ofurea. J. Am. Chem. Soc. 124, 1192-1202.

Zou, Q., Habermann-Rottinghaus, S. M., and Murphy, K. P. (1998). Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect. Proteins Struct. Funct. Genet. 31, 107-115.

Was this article helpful?

0 0

Post a comment