References: Standard pKa values Cantor, C.R. and Schimmel, P.R., "Biophysical Chemistry, Part I," W.H. Freeman, San Francisco, p. 49 (1980). Hydrophobicity chart Lesser, G.J., Lee, R.H., Zehfus, M.H., and Rose, G.D., "Hydrophobic Interactions in Proteins," in Protein Engineering (Oxender, D.L. and Fox, C.F., eds.) Alan R. Liss, New York, pp. 175-179 (1987). Chou-Fasman helix/sheet propensities Prevelige, P. Jr. and Fasman, G.D., "Chou-Fasman Prediction of the Secondary Structure of Proteins," in Prediction of Protein Structure and The Priniciples of Protein Conformation (Fasman, G.D., ed.) Plenum Press, New York, pp. 391-416 (1989). Chou, P.Y. and Fasman, G.D., "Prediction of Protein Conformation," Biochemistry 13, 222-245 (1974). Molecular weights and chemical composition "The Merck Index," (Budavari, S., ed.) Merck & Co., Rahway, (1989). Amino acid codons Stryer, L., "Biochemistry," W.H. Freeman, San Francisco, p. 629 (1975). Sequential and medium-range proton distances in polypeptide secondary structures Wuthrich, K., "NMR of Proteins and Nucleic Acids," John Wiley & Sons, New York, p. 127 (1986). Secondary structure backbone proton-proton NOE intensities and secondary structure H-alpha to NH coupling constants Wuthrich, K., "NMR of Proteins and Nucleic Acids," John Wiley & Sons, New York, p. 166 (1986). Wagner, G., Neuhaus, D., Worgotter, E., Vasak, M., Kagi, J.R.H., and Wuthrich, K., "Nuclear Magnetic Resonance Identification of 'Half- turn' and 3-10- Helix Secondary Structure in Rabbit Liver Metallothionein-2," J. Mol. Biol. 187, 131-135 (1986). Chemical shift index calculations Wishart, D.S. and Sykes, B.D., "The 13C Chemical-Shift Index: A Simple Method for the Identification of Protein Secondary Structure Using 13C Chemical-Shift Data," J. Biomol. NMR 4, 171-180 (1994). Wishart, D.S., Sykes, B.D., and Richards, F.M., "Chemical Shift Index: A Fast and Simple Method for the Assignment of Protein Secondary Structure through NMR Spectroscopy," Biochemistry 31, 1647-1651.