Theory Department
Max Planck Institute of Microstructure Physics
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Yitamben, E. N., Niebergall, L., Rankin, R. B., Iski, E. V., Rosenberg, R. A., Greeley, J. P., Stepanyuk, V. S., Guisinger, N. P.

Tracking amino acids in chiral quantum corrals
The Journal of Physical Chemistry C 117, (22),pp 11757-11763 (2013)
Molecular diffusion, motion, and conformation are critical to chemical and biological processes. Concurrently, understanding how chirality affects these processes has become a critical challenge for various applications in the pharmaceutical and food industries ranging from drug catalysis to novel sensing. Here, we present a unique way of transferring the chirality of simple amino acids, L- and D-alanine, to large-scale chiral networks on Cu(111). We further utilize the unique geometry of the chiral network as a scaffolding to isolate individual molecules within a 1.2 nm hexagonal pore. These hexagonal pores act as single molecule \'race tracks\'where excess alanine molecules trapped at the perimeter are observed to hop between six distinct locations around the perimeter. Scanning tunneling microscopy (STM) as well as density functional theory (DFT) calculations have been utilized to directly track, influence, and probe this molecular motion confined to self-assembled, chiral, hexagonal pores which also form quantum corrals.

TH-2013-17