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Science 10 July 1998:
Vol. 281. no. 5374, pp. 253 - 256
DOI: 10.1126/science.281.5374.253
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Reports

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

Tanja Kortemme, *dagger Marina Ramírez-Alvarado, *dagger Luis Serrano

A 20-residue protein (named Betanova) forming a monomeric, three-stranded, antiparallel beta  sheet was designed using a structural backbone template and an iterative hierarchical approach. Structural and physicochemical characterization show that the beta -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 beta -sheet formation, including beta -sheet aggregation and amyloid fibril formation.

European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, Heidelberg D-69117, Germany.
*   These authors contributed equally to this work.

dagger    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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