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- Title
Design of a 20-amino acid, three-stranded beta-sheet protein.
- Authors
Kortemme, T; Ramírez-Alvarado, M; Serrano, L
- 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.
- Publication
Science (New York, N.Y.), 1998, Vol 281, Issue 5374, p253
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.281.5374.253