TY - JOUR
T1 - Design of a 20-amino acid, three-stranded β-sheet protein
AU - Kortemme, Tanja
AU - Ramírez-Alvarado, Marina
AU - Serrano, Luis
PY - 1998/7/10
Y1 - 1998/7/10
N2 - 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.
AB - 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.
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U2 - 10.1126/science.281.5374.253
DO - 10.1126/science.281.5374.253
M3 - Article
C2 - 9657719
AN - SCOPUS:2642670311
SN - 0036-8075
VL - 281
SP - 253
EP - 256
JO - Science
JF - Science
IS - 5374
ER -