Atomic force microscopy (AFM) can be used to study biomolecules that have been bound to a mica surface.  The genetic processes and molecular signaling in cells are thought to be greatly impacted by the structures of DNA and proteins.  When AFM is used at a high enough resolution, the detailed structure of DNA and proteins can be studied.  Here we used AFM to visualize the structural change between supercoiled and linear pUC19.  In addition, we investigated the properties of immobilized calmodulin (CaM) on different modified mica and in different conditions using AFM.  Ca2+ binding to CaM causes a conformational change, exposing its hydrophobic residues, which allows it to recognize different target proteins.  The AFM characterization will provide insight into protein properties at the interface between aqueous and solid phases.  This project was supported by National Science Foundation grant DUE-0633186 and the SIUE Undergraduate Research and Creative Activities Program.

AFM imaging analysis of pUC19 DNA and calmodulin

243rd National Meeting (2012)

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