Evolutionary design of glutathione-linked proteins in vivo and in vitro based on sampling of modules from pre-existing structures
Structural studies suggest that naturally occurring proteins represent a limited number of folds. It would appear that the evolution of novel protein functions to a large extent involves redesign of stable peptide scaffolds by means of combinatorial prote
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Veröffentlicht in: | Chemico-biological interactions 2001-02, Vol.133 (1-3), p.3 |
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Hauptverfasser: | , , , , , , , , , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | Structural studies suggest that naturally occurring proteins represent a limited number of folds. It would appear that the evolution of novel protein functions to a large extent involves redesign of stable peptide scaffolds by means of combinatorial prote |
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ISSN: | 0009-2797 |
DOI: | 10.1016/S0009-2797(00)00216-7 |