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Publication Detail
A recurring theme in protein engineering: the design, stability and folding of repeat proteins
  • Publication Type:
    Journal article
  • Publication Sub Type:
    JOUR
  • Authors:
    Main ER, Lowe AR, Mochrie SG, Jackson SE, Regan L
  • Publication date:
    2005
  • Pagination:
    464, 471
  • Journal:
    Curr Opin Struct Biol
  • Volume:
    15
  • Medium:
    4
  • Print ISSN:
    0959-440X
  • Keywords:
    Humans Models, Molecular Protein Binding Protein Conformation Protein Engineering Protein Folding
  • Notes:
    Main, Ewan R G Lowe, Alan R Mochrie, Simon G J Jackson, Sophie E Regan, Lynne Research Support, Non-U.S. Gov't Review Current opinion in structural biology S0959-440X(05)00125-9 [pii] Curr Opin Struct Biol. 2005 Aug;15(4):464-71. Repeat proteins are ubiquitous and are involved in a myriad of essential processes. They are typically non-globular structures that act as diverse scaffolds for the mediation of protein-protein interactions. These excitingly different structures, which arise from tandem arrays of a repeated structural motif, have generated significant interest with respect to protein engineering and design. Recent advances have been made in the design and characterisation of repeat proteins. The highlights include re-engineering of binding specificity, quantitative models of repeat protein stability and kinetic studies of repeat protein folding.
Abstract
Repeat proteins are ubiquitous and are involved in a myriad of essential processes. They are typically non-globular structures that act as diverse scaffolds for the mediation of protein-protein interactions. These excitingly different structures, which arise from tandem arrays of a repeated structural motif, have generated significant interest with respect to protein engineering and design. Recent advances have been made in the design and characterisation of repeat proteins. The highlights include re-engineering of binding specificity, quantitative models of repeat protein stability and kinetic studies of repeat protein folding.
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