The central dogma of protein science has been that proteins require structure to be functional.  However, intrinsically disordered proteins (IDPs) are a class of proteins that do not have a specific conformation.  IDPs typically become ordered upon binding to their target protein, though there are still many questions regarding how IDPs recognize their targets.  Previous studies showed the disordered phenotype was not conserved between homologous IDPs.  This study compares the binding constants between the antisigma factor FlgM and sigma-28 from different strains of bacteria. By measuring binding between FlgM from one strain and sigma-28 of another, this study determines if differing degrees of disorder allow for flexibility in binding partners.  Using disorder predictions, isothermal calorimetry, and fluorescence spectroscopy, the results will determine different binding affinities exhibited by FlgM.

Comparison of binding between intrinsically disordered homologous FlgM proteins to determine structural homology

243rd National Meeting (2012)

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