A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix(286 views) Ronga L, Palladino P, Ragone R, Benedetti E, Rossi F
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Santoro, M. M., Bolen, D. W., Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants (1988) Biochemistry, 27, pp. 8063-8068
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Bordbar, A. K., Saboury, A. A., Housaindokht, M. R., Moosavi-Movahedi, A. A., Statistical effects of the binding of ionic surfactant to protein (1997) J. Colloid Interface Sci, 192, pp. 415-419
Nelson, J. W., Kallenbach, N. R., Stabilization of the ribonuclease S-peptide -helix by trifluoroethanol (1986) Proteins, 1, pp. 211-217
Sch nbrunner, N., Wey, J., Engels, J., Georg, H., Kiefhaber, T., Native-like -structure in a trifluoroethanol-induced partially folded state of the all- -sheet protein tendamistat (1996) J. Mol. Biol, 260, pp. 432-445
Yang, J. T., Wu, C. S. C., Martinez, H. M., Calculation of protein conformation from circular dichroism (1986) Methods Enzymol, 130, pp. 208-269
Wu, J. W., Wang, Z. X., New evidence for the denaturant binding model (1999) Protein Sci, 8, pp. 2090-2097
Schellman, J. A., Selective binding and solvent denaturation (1987) Biopolymers, 26, pp. 549-559
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Borchelt, D. R., Taraboulos, A., Prusiner, S. B., Evidence for synthesis of scrapie prion proteins in the endocytic pathway (1992) J. Biol. Chem, 267, pp. 16188-16199
Knaus, K. J., Morillas, M., Swietnicki, W., Malone, M., Surewicz, W. K., Yee, V. C., Crystal structure of the human prion protein reveals a mechanism for oligomerization (2001) Nat. Struct. Biol, 8, pp. 770-774
A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix