Dramatic Shape Changes Occur as Cytochrome c Folds.

ABSTRACT: Extensive experimental studies on the folding of cytochrome c (Cyt c) make this small protein an ideal target for atomic detailed simulations for the purposes of quantitatively characterizing the structural transitions and the associated time scales for folding to the native state from an ensemble of unfolded states. We use previously generated atomically detailed folding trajectories by the stochastic difference equation in length to calculate the time-dependent changes in the small-angle X-ray scattering (SAXS) profiles. Excellent agreement is obtained between experiments and simulations for the time-dependent SAXS spectra, allowing us to identify the structures of the folding intermediates, which shows that Cyt c reaches the native state by a sequential folding mech

SUBMITTER: Kirmizialtin S 

PROVIDER: S-EPMC7908931 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature