Science. 1998 Jul 10;281(5374):253-6.

Design of a 20-amino acid, three-stranded beta-sheet protein.

Kortemme T, Ramírez-Alvarado M, Serrano L.

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European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, Heidelberg D-69117, Germany.

Abstract

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.

PMID:: 9657719; [PubMed - indexed for MEDLINE]

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Design of a 20-amino acid, three-stranded beta-sheet protein.

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