Design of a 20-amino acid, three-stranded beta-sheet protein.
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Summary
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.
- Type
- article
- Published
- 1998-07-10
- Cited by
- 58
- References
- 0
- OpenAlex
- https://openalex.org/W2069852256
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:27919804
Keywords
Antiparallel (mathematics), Beta sheet, Monomer, Protein folding, Chemistry
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