Effect of Weakly Interacting Cosolutes on Lysozyme Conformations.

ABSTRACT: Exposure of a protein to cosolutes, like denaturants, changes its folding equilibrium. To determine the ensemble of protein conformations at equilibrium, in the presence of weakly interacting cosolutes, we present a two-stage analysis of solution X-ray scattering data. In the first stage, Guinier analysis and Kratky plot revealed information about the compactness and flexibility of the protein. In the second stage, elastic network contact model and coarse-grained normal mode analysis were used to generate an ensemble of conformations. The scattering curves of the conformations were computed and fitted to the measured scattering curves to get insights into the dominating folding states at equilibrium. Urea and guanidine hydrochloride (GuHCl) behaved as preferentially included weakly interac

SUBMITTER: Levartovsky Y 

PROVIDER: S-EPMC6643829 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature