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.
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Gilmanshin, R., Callender, R. & Dyer, R. The core of apomyoglobin E-form folds at the diffusion limit. Nat Struct Mol Biol 5, 363–365 (1998). https://doi.org/10.1038/nsb0598-363
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DOI: https://doi.org/10.1038/nsb0598-363
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