Affiliation:
1. European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, Heidelberg D-69117, Germany.
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.
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
320 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献