Abstract
The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15–20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 μs at 46 °C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation.
Original language | English (US) |
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Pages (from-to) | 363-365 |
Number of pages | 3 |
Journal | Nature Structural Biology |
Volume | 5 |
Issue number | 5 |
DOIs | |
State | Published - May 1998 |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics