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Regensburg 2013 – scientific programme

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BP: Fachverband Biologische Physik

BP 8: Posters: Proteins

BP 8.1: Poster

Monday, March 11, 2013, 17:30–19:30, Poster B2

Effects of ligand binding on cyclophilin A: experimental and computational studies — •Jack Heal1, Stephen Wells2, Claudia Blindauer3, Rudolf Römer2, and Robert Freedman41MOAC Doctoral Training Center, University of Warwick, Coventry, UK, CV4 7AL — 2Department of Physics, University of Warwick, Coventry, UK, CV4 7AL — 3Department of Chemistry, University of Warwick, Coventry, UK, CV4 7AL — 4Department of Life Sciences, University of Warwick, Coventry, UK, CV4 7AL

Cyclophilin A is an enzyme which plays a role in the folding of proteins. It also binds to and aids the function of the immunosuppressant drug cyclosporin A as well as binding to the HIV-1 capsid protein. We use the computational tools FIRST and FRODA to model the flexibility and motion of cyclophilin A in order to predict the results of hydrogen-deuterium exchange NMR (HDX) experiments. The rigidity analysis software FIRST can be used to predict the `folding cores' of proteins identified as slowly exchanging residues in HDX. This prediction is improved using the protein mobility software FRODA. We are using these methods to investigate the effect of ligand binding on cyclophilin A computationally and experimentally.

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