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Engineering of zinc finger and MHC motifs to locked-in tertiary folds

Mathieu, Marc ; Lehmann, Christian ; Razaname, Alain ; Tuchscherer, Gabriele

In: Letters in Peptide Science, 1997, vol. 4, no. 2, p. 95-100

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    Titre
    • Engineering of zinc finger and MHC motifs to locked-in tertiary folds
    Auteur
    • Mathieu, Marc. Institute of Organic Chemistry, University of Lausanne, BCH-Dorigny, CH- 1015, Lausanne, Switzerland
    • Lehmann, Christian. Institute of Organic Chemistry, University of Lausanne, BCH-Dorigny, CH- 1015, Lausanne, Switzerland
    • Razaname, Alain. Institute of Organic Chemistry, University of Lausanne, BCH-Dorigny, CH- 1015, Lausanne, Switzerland
    • Tuchscherer, Gabriele. Institute of Organic Chemistry, University of Lausanne, BCH-Dorigny, CH- 1015, Lausanne, Switzerland
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • Letters in Peptide Science, 1997, vol. 4, no. 2, p. 95-100. Kluwer Academic Publishers
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:312503
    Summary
    The assembly of helical and β-sheet peptide blocks containing reactive chain ends results inhighly branched chain architectures (‘locked-in folds') mimicking native tertiary structures.This molecular kit strategy allows to bypass the protein folding problem in protein de novodesign and gives access to protein mimetics of high thermodynamic stability. The validity ofthis concept is exemplified for the design and synthesis of locked-in folds mimicking the zincfinger and MHC folding motifs