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References

  • Adler, M. and Scheraga, H.A. 1990. Nonnative isomers of proline-93 and -114 predominate in the heat-unfolded ribonuclease A. Biochemistry 29: 82118216.
  • Alexandrescu, A.T., Rathgeb-Szbo, K., Rumpel, K., Jahnke, W., Schulthess, T., and Kammerer, R. 1998. 15N backbone dynamics of the S-peptide from ribonuclease A in its free and S-protein bound forms: Toward a site-specific analysis of entropy changes upon folding. Protein Sci. 7: 389402.
  • Biringer, R.G. and Fink, A.L. 1982. Observation of intermediates in the folding of ribonuclease A at low temperature using proton nuclear magnetic resonance. Biochemistry 21: 47484755.
  • Cavanagh, J., Fairbrother, W.J., Palmer III, A.G., and Skelton, N.J. 1995. Protein NMR spectroscopy. Academic Press, London.
  • Jaenicke, R. and Rudolph, R. 1989. Folding proteins. In Protein structure, a practical approach. (ed. T.E.Creighton), pp. 191224. IRL Press, New York.
  • Jones, D.S. 1979. Elementary information theory. Oxford University Press, Oxford.
  • Laity, J.H., Lester, C.C., Shimotakahara, S., Zimmerman, D.E., Montelione, G.T., and Scheraga, H.A. 1997. Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A. Biochemistry 36: 1268312699.
  • Li, Y.J., Rothwarf, D.M., and Scheraga, H.A. 1995. Mechanism of reductive protein unfolding. Nat. Struct. Biol. 20 2: 489494.
  • McDonald, C.C. and Phillips, W.D. 1967. Manifestations of the tertiary structures of proteins in high-frequency nuclear magnetic resonance. J. Am. Chem. Soc. 89: 63326341.
  • McDonald, R.S. and Wilks, P.A. 1988. JCAMP-DX: A standard form for exchange of infrared spectra in computer readable form. Appl. Spectrosc. 42: 151162.
  • Neira, J.L. and Rico, M. 1997. Folding studies on ribonuclease A, a model protein. Fold. & Des. 2: R1R11.
  • Ohya, M. and Petz, D. 1993. Quantum entropy and its use. Springer-Verlag, Heidelberg.
  • Pace, N.C., Shirley, B.A., and Thomson, J.A. 1989. Measuring the conformational stability of a protein. In Protein structure, a practical approach. (ed. T.E.Creighton), pp. 311330. IRL Press, New York.
  • Rico, M., Bruix, M., Santoro, J., Gonzales, C., Neira, J.L., Nieto, J.L., and Herranz, J. 1989. Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A. Eur. J. Biochem. 183: 623638.
  • Robertson, A.D., Purisima, E.O., Eastman, M.A., and Scheraga, H.A. 1989. Proton NMR assignment and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution. Biochemistry 28: 59305938.
  • Rothwarf, D.M. and Scheraga, H.A. 1993a. Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution. Biochemistry 32: 26712679.
  • Rothwarf, D.M. and Scheraga, H.A. 1993b. Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration. Biochemistry 32: 26802689.
  • Rothwarf, D.M. and Scheraga, H.A. 1993c. Regeneration of bovine pancreatic ribonuclease A. 3. Dependence on the nature of the redox reagent. Biochemistry 32: 26802689.
  • Santoro, J., González, C., Bruix, M., Neira, J.L., Nieto, J.L., Herranz, J., and Rico, M. 1993. High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 229: 722734.
  • Shimotakahara, S., Rios, C.B., Laity, J.H., Zimmerman, D.E., Scheraga, H.A., and Montelione, G.T. 1997. NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: Automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms. Biochemistry 36: 69156929.
  • Smith, L.J., Bolin, K.A., Schwalbe, H., MacArthur, M.W., Thornton, J.M., and Dobson, C.M. 1996. Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 255:494506.
  • Talluri, S., Rothwarf, D.M., and Scheraga, H.A. 1994. Structural characterization of a three-disulfide intermediate of robonuclease A involved in both folding and unfolding pathways. Biochemistry 33: 1043710449.
  • Wagner, G. 1997. An account of NMR in structural biology. Nat. Struct. Biol., NMR Suppl. 10: 841844.
  • Williams, R.J.P. 1989. NMR studies of mobility within protein structure. Eur. J. Biochem. 183: 479497.
  • Wishart, D.S., Sykes, B.D., and Richards, F.M. 1991. Relationship between nuclear magnetic resonance chemical shifts and protein secondary structure. J. Mol. Biol. 222: 311333.
  • Zhang, J., Peng, X.D., Jonas, A., and Jonas, J. 1995. NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry 34: 86318641.