Abstract
New studies have shown that folding of β-sheet proteins can occur with and without intermediates, with fast to slow refolding rates and late to very late transition states. These experiments demonstrate that, despite early speculation to the contrary, β-sheet protein folding does not appear to be fundamentally different from that of helical and mixed α,β proteins.
Original language | English (US) |
---|---|
Pages (from-to) | 86-92 |
Number of pages | 7 |
Journal | Current Opinion in Structural Biology |
Volume | 8 |
Issue number | 1 |
DOIs | |
State | Published - Feb 1998 |
Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology