Sequence space, folding and protein design

Matthew H.J. Cordes, Alan R. Davidson, Robert T. Sauer

Research output: Contribution to journalArticle

139 Scopus citations

Abstract

Protein design efforts are beginning to yield molecules with many of the properties of natural proteins. Such experiments are informed by and contribute to our understanding of the sequence determinants of protein folding and stability. The most important design elements seem to be the proper placement of hydrophobic residues along the polypeptide chain and the ability of these residues to form a well packed core. Buried polar interactions, turn and capping motifs and secondary structural propensities also contribute, although probably to a lesser extent.

Original languageEnglish (US)
Pages (from-to)3-10
Number of pages8
JournalCurrent Opinion in Structural Biology
Volume6
Issue number1
DOIs
StatePublished - Feb 1996
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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