Characterization of folding cores in the cyclophilin A-cyclosporin A complex.

ABSTRACT: Determining the folding core of a protein yields information about its folding process and dynamics. The experimental procedures for identifying the amino acids that make up the folding core include hydrogen-deuterium exchange and Φ-value analysis and can be expensive and time consuming. Because of this, there is a desire to improve upon existing methods for determining protein folding cores theoretically. We have obtained HDX data for the complex of cyclophilin A with the immunosuppressant cyclosporin A. We compare these data, as well as literature values for uncomplexed cyclophilin A, to theoretical predictions using a combination of rigidity analysis and coarse-grained simulations of protein motion. We find that in this case, the most specific prediction of folding cores comes from a co

SUBMITTER: Heal JW 

PROVIDER: S-EPMC4390823 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature