A Review of Methods for Protein Structure Comparison View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1992

AUTHORS

Christine A. Orengo

ABSTRACT

As increasing numbers of structures are determined and compared, it has become apparent that there are extensive similarities in the chain fold (or topology) of many proteins. In recent years techniques have been developed which attempt to predict, or model, the structure of a protein from the amino acid sequence by utilising these common structural elements. In addition to identifying recurring topologies, structure comparisons have also revealed smaller structural fragments or motifs accross a wide range of proteins; for example, the βαβ and the β-hairpin motifs (see Thornton et al., in this Vol.). Characterising these motifs in terms of geometry, distance constraints and sequence composition can enhance protein structure prediction techniques by incorporating longer range interactions between secondary structures. More... »

PAGES

159-188

References to SciGraph publications

  • 1989-01. The alignment of protein structures in three dimensions in BULLETIN OF MATHEMATICAL BIOLOGY
  • 1988-12. A flexible method to align large numbers of biological sequences in JOURNAL OF MOLECULAR EVOLUTION
  • 1977-12. Recognition of phylogenetic relationships from polypeptide chain fold similarities in JOURNAL OF MOLECULAR EVOLUTION
  • Book

    TITLE

    Patterns in Protein Sequence and Structure

    ISBN

    978-3-642-76639-8
    978-3-642-76637-4

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/978-3-642-76637-4_16

    DOI

    http://dx.doi.org/10.1007/978-3-642-76637-4_16

    DIMENSIONS

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