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Protein Structure Prediction pp 71–95Cite as

Third Generation Prediction of Secondary Structures

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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 143))

Abstract

The sequence-structure gap is rapidly increasing. Currently, databases for protein sequences (e.g., SWISS-PROT [1]) are expanding rapidly, largely due to large-scale genome sequencing projects: at the beginning of 1998, we know already all sequences for a dozen of entire genomes (2). This implies that despite significant improvements of structure determination techniques, the gap between the number of protein structures in public databases (PDB [3]), and the number of known protein sequences is increasing. The most successful theoretical approach to bridging this gap is homology modeling. It effectively raises the number of “known” 3D structures from 7000 to over 50,000 (4,5).

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Author information

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY

    Burkhard Rost

  2. Millenium Bioinformatics, Boston, MA

    Chris Sander

Authors
  1. Burkhard Rost
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  2. Chris Sander
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Editor information

Editors and Affiliations

  1. Southern Cross Molecular, Freshford, Bath, UK

    David M. Webster

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© 2000 Humana Press Inc.

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Rost, B., Sander, C. (2000). Third Generation Prediction of Secondary Structures. In: Webster, D.M. (eds) Protein Structure Prediction. Methods in Molecular Biology™, vol 143. Humana Press. https://doi.org/10.1385/1-59259-368-2:71

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  • DOI: https://doi.org/10.1385/1-59259-368-2:71

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-637-6

  • Online ISBN: 978-1-59259-368-2

  • eBook Packages: Springer Protocols

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