With the goal to facilitate the global multi-method analysis (GMMA) of biophysical protein interactions data, we have embarked on the application of isothermal titration calorimetry (ITC) to the study of self-associating proteins. Such experiments have been difficult in the past, but our initial results using a model system promises significant improvement using global and multi-method modelling approaches as implemented in our software SEDPHAT. Separately, for the reliable analysis of protein interaction data acquired with surface plasmon resonance biosensors, we have updated our detailed protocol and published a review with emphasis on the heterogeneity of binding sites often created by surface immobilization. Finally, in order to disseminate our GMMA software and facilitate its application by colleagues, we have held multiple workshops at NIH in Bethesda, which have generated positive feedback and software improvements.
