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Design of a 20-Amino Acid, Three-Stranded β-Sheet Protein

Science  10 Jul 1998:
Vol. 281, Issue 5374, pp. 253-256
DOI: 10.1126/science.281.5374.253

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Abstract

A 20-residue protein (named Betanova) forming a monomeric, three-stranded, antiparallel β sheet was designed using a structural backbone template and an iterative hierarchical approach. Structural and physicochemical characterization show that the β-sheet conformation is stabilized by specific tertiary interactions and that the protein exhibits a cooperative two-state folding-unfolding transition, which is a hallmark of natural proteins. The Betanova molecule constitutes a tractable model system to aid in the understanding of β-sheet formation, including β-sheet aggregation and amyloid fibril formation.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: Kortemme{at}EMBL-Heidelberg.DE (T.K.) and Ramirez{at}EMBL-Heidelberg.DE (M.R.-A.).

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