We're a molecular biophysics laboratory primarily interested in the relationships between protein structure and function. In particular we are focused on intrinsically disordered regions and how they impact function.

The laboratory is studying the regulation of the Ser/Thr phosphatase calcineurin. Calcineurin is activated when bound by the calcium-sensor protein calmodulin. This system is rich in disorder and is an ideal model system for studying the relationship between disorder and function. Not only is the regulatory domain of calcineurin disordered, some proteins that directly regulate calcineurin also possess disorder. We employ a range of biophysical techniques to study calcineurin regulation in vitro, including fluorescence, circular dichroism, NMR and analytical centrifugation. To learn more, click on the Research tab above.

Calmodulin binds to and regulates a great many proteins including calcineurin. It has been suggested that calmodulin binds to disordered regions within these proteins. Consequently we are interested in other calmodulin targets. To learn more, click on the Research tab above.