Intrinsically disordered proteins (IDPs) are becoming a focus of research as principal players of key ultra-molecular self-assembly and regulatory cellular events. To elucidate the molecular mechanisms of interactions of IDPs with their partners, it is important to structurally characterize these proteins both in isolation and in complexes. Atomic Force Microscopy (AFM) may have a potential in delivering images of IDPs at molecular resolution. Until now, no static AFM images of IDPs in isolation were published. Here we present AFM imaging of a 510-residue N-terminal, disordered region of protein supervillin known to be associated with lipid membranes and capable of binding f-actin and myosin II. Our results suggest that AFM imaging can be used for structural characterization of IDRs in isolation and in complexes. A potential advantage of such recording over the recently introduced high-speed AFM can be a higher resolution of images for larger, less dynamic IDRs.

AFM imaging of Supervillin fragments details an unfolded structure

243rd National Meeting (2012)

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