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Letter
Nature Structural & Molecular Biology 5, 363–365 (1 May 1998) | doi:10.1038/nsb0598-363
The core of apomyoglobin E-form folds at the diffusion limit
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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 |[mu]|s at 46 |[deg]|C, close to the diffusion limit for loop formation.
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