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

نویسندگان

  • Jack W Heal
  • Stephen A Wells
  • Claudia A Blindauer
  • Robert B Freedman
  • Rudolf A Römer
چکیده

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 combined approach that models the rigidity of the protein using the first software suite and the dynamics of the protein using the froda tool.

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عنوان ژورنال:
  • Biophysical journal

دوره 108 7  شماره 

صفحات  -

تاریخ انتشار 2015