Design of a 20-Amino Acid, Three-Stranded β-Sheet Protein
1998; American Association for the Advancement of Science; Volume: 281; Issue: 5374 Linguagem: Inglês
10.1126/science.281.5374.253
ISSN1095-9203
AutoresTanja Kortemme, Marina Ramı́rez-Alvarado, Luís Serrano,
Tópico(s)Alzheimer's disease research and treatments
ResumoA 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.
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