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

Tanja Kortemme, Marina Ramírez-Alvarado, Luis Serrano

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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.

Original languageEnglish (US)
Pages (from-to)253-256
Number of pages4
JournalScience
Volume281
Issue number5374
DOIs
StatePublished - Jul 10 1998

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