The core of apomyoglobin E-form folds at the diffusion limit.
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 micros at 46 degrees 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.
Gilmanshin
R
R
Callender
R H
RH
Dyer
R B
RB
D000818:Animals; D001059:Apoproteins / Q000737:chemistry*; D004058:Diffusion; D006736:Horses; D009211:Myoglobin / Q000737:chemistry*; D017510:Protein Folding; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin