Abstract
To predict the secondary structure of soluble proteins several schemes are available (see other chapters in this book). Most of them are variations and extensions of the same principle developed by Chou and Fasman (1974). To each amino acid residue one attributes a potential for α-helix, β-strand, and β-turn conformation, which has been deduced from proteins of known three-dimensional structure. For a protein of unknown structure, the profiles of the three potentials along the amino acid sequence are compared to predict the secondary structure. The predictive power of such an analysis is limited, but in many cases this is the sole piece of structural information available.
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© 1989 Plenum Press, New York
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Jähnig, F. (1989). Structure Prediction for Membrane Proteins. In: Fasman, G.D. (eds) Prediction of Protein Structure and the Principles of Protein Conformation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1571-1_18
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DOI: https://doi.org/10.1007/978-1-4613-1571-1_18
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