Equilibrium folding dynamics of meACP in water, heavy water, and low concentration of urea.

ABSTRACT: Many proteins fold in apparent two-state behavior, as partially folded intermediates only transiently accumulate and easily escape detection. Besides a native form and a mainly unfolded form, we captured a partially unfolded form of an acyl carrier protein from Micromonospora echinospora (meACP) in the folding/unfolding equilibrium using chemical exchange saturation transfer NMR experiments. The C-terminal region of the partially unfolded form is mainly folded and the N-terminal is unfolded. Furthermore, to understand how the folding process of meACP is influenced by solvent environments, we compared the folding dynamics of meACP in D₂O, H₂O and low concentration of urea. As the environment becomes more denaturing from D₂O to H₂O and then to urea

SUBMITTER: Zhou Y 

PROVIDER: S-EPMC5700953 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature