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A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules

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References:


Standard pKa values

    Cantor, C.R. and Schimmel, P.R., "Biophysical Chemistry, Part I," 
    W.H. Freeman, San Francisco, p. 49 (1980).

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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