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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.

Keywords

Membrane Plane Amphipathic Helix Hydrophobic Moment Lactose Permease Helical Wheel 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Fritz Jähnig
    • 1
  1. 1.Max Planck Institute for BiologyTübingenWest Germany

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