| AVS 58th Annual International Symposium and Exhibition | |
| Biomaterial Interfaces Division | Monday Sessions |
| Session BI-MoM |
| Session: | Biomolecules at Interfaces |
| Presenter: | Sajida Khan, Ohio University |
| Authors: | S. Khan, Ohio University K. Clark, Ohio University C. Henneken, Ohio University E. Rauh, Ohio University S.-W. Hla, Ohio University |
| Correspondent: | Click to Email |
Scanning tunneling microscope (STM) is not only an instrument to image atomic landscape of material surfaces but also is a tool to manipulate individual atoms and molecules. If STM manipulation and spectroscopy can be applied to individual biomolecules, it will be advantageous for multiple research areas. Here we use a low temperature STM in an ultrahigh environment to image individual protein molecules with molecular resolution on Ag (111) surface at 4.6 K. A-b type amyloid precursor proteins molecules and various single chain proteins were deposited on atomically clean Ag (111) surface. STM images and tunneling spectroscopy enables direct sequencing of amino acid groups in these molecules. Moreover, using an STM manipulation procedure employing an attractive tip-molecule interaction, individual molecules were relocated on the surface; thereby their mechanical integrity can be tested. Protein folding is a major issue in biological processes. Here, we will demonstrate that folding of carbon back-bone in these proteins is possible using an STM manipulation procedure. This experiment presents a novel avenue of biological research where sequencing and manipulation may be performed one molecule-at-a-time. We acknowledge the financial support provided by US-DOE-DE-FG02-02ER46012.