Betanova
A 20-residue protein 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.
Bursulaya and Brooks J. Am. Chem. Soc. (1999) 121: 9947-9951
Kortemme, Ramirez-Alvarado, & Serrano, Science (1998) 281: 253-256