Standard pKa values
Cantor, C.R. and Schimmel, P.R., "Biophysical Chemistry, Part I,"
W.H. Freeman, San Francisco, p. 49 (1980).
Updated pKa for Asp and Glu
"Measurement of side-chain carboxyl pK(a) values of glutamate and
aspartate residues in an unfolded protein by multinuclear NMR spectroscopy."
Tollinger M, Forman-Kay JD, Kay LE.
J Am Chem Soc. 2002 May 22;124(20):5714-7.
Updated pKa for Lys
"Residue-specific pKa determination of lysine and arginine side chains by
indirect 15N and 13C NMR spectroscopy: application to apo calmodulin.
André I, Linse S, Mulder FA.
J Am Chem Soc. 2007 Dec 26;129(51):15805-13. Epub 2007 Nov 29.
Updated pKa for Tyr
"C-13 Nuclear Magnetic-Resonance Study of Tyrosine Titrations"
Norton RS, Bradbury JH"
Journal of the Chemical Society-Chemical Communications Issue: 21
Pages: 870-871 Published: 1974
pI and Amino Acid Occurence:
Nelson, D. L and Cox, M. M., "Lehninger Principles of Biochemistry,
Third Edition," Worth Publishers, New York, p. 118 (2000)
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.
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