A protein folding pathway with multiple folding intermediates at atomic resolution
AUTOR(ES)
Feng, Hanqiao
FONTE
National Academy of Sciences
RESUMO
Using native-state hydrogen-exchange-directed protein engineering and multidimensional NMR, we determined the high-resolution structure (rms deviation, 1.1 Å) for an intermediate of the four-helix bundle protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix and a part of the C-terminal helix unfolded. In earlier studies, we also solved the structures of two other folding intermediates for the same protein: one with the N-terminal helix alone unfolded and the other with a reorganized hydrophobic core. Together, these structures provide a description of a protein folding pathway with multiple intermediates at atomic resolution. The two general features for the intermediates are (i) native-like backbone topology and (ii) nonnative side-chain interactions. These results have implications for important issues in protein folding studies, including large-scale conformation search, φ-value analysis, and computer simulations.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=555603Documentos Relacionados
- Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
- The folding pathway of a protein at high resolution from microseconds to seconds
- Probing the antibody-catalyzed water-oxidation pathway at atomic resolution
- Intermediates can accelerate protein folding
- A minimalist model protein with multiple folding funnels