Single-Molecule Analysis with Nanomechanical Systems

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Date 06.09.2016
Hour 11:0012:00
Speaker Prof. Michael Roukes, Caltech
Bio: Michael Roukes is the Robert M. Abbey Professor of Physics, Applied Physics, and Bioengineering at the California Institute of Technology.  His scientific interests range from quantum measurement to applied biotechnology with a unifying theme of the development, very-large-scale integration and application of complex nanosystems to precision measurements in physics, the life sciences and medicine.  Roukes was the founding Director of Caltech's Kavli Nanoscience Institute (KNI) from 2003-2006.  In 2007, he co-founded the Alliance for Nanosystems VLSI (very-large-scale integration) with scientists and engineers at CEA/LETI in Grenoble, which maintains a $B-scale microelectronics research foundry.  He then continued as co-director of Caltech’s KNI from 2008 until 2013. Since then he has returned to full-time pursuit of research efforts with his group and collaborators. Concurrent with his Caltech appointment, he has held a Chaire d’Excellence in nanoscience in Grenoble, France since 2008.  Among his honors, Roukes is a recipient of the NIH Director’s Pioneer Award and has been awarded Chevalier (Knight) dans l'Ordre des Palmes Academiques by the Republic of France.
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Category Conferences - Seminars
NEMS (nanoelectromechanical systems) now enable ultrasensitive measurement of the inertial mass of individual atoms and molecules [1]. We have employed NEMS devices to realize a new form of mass spectrometry (MS) enabling single-molecule analysis, and with it have analyzed individual large-mass biomolecular complexes, one-by-one, in real-time [2]. Recently, we developed an approach that enhances our previously demonstrated capabilities of NEMS-MS by resolving the spatial mass distribution of the individual analytes – in real time with molecular-scale resolution – upon their adsorption onto the NEMS sensor [3]. This new approach, which we term inertial imaging, employs the ensemble of discrete time-correlated perturbations, resulting from each molecular adsorption event, to yield the spatial moments of the mass distribution in real time for each analyte. The lowest moment yields the analyte’s total mass; higher moments reveal its center-of-mass position of adsorption, the analyte’s average diameter, and its spatial skew and kurtosis, etc. Once acquired, these moments can be employed to reconstruct the analyte’s “inertial image”. Unlike conventional imaging, the precision of inertial imaging is not set by wavelength-dependent diffraction phenomena; instead frequency fluctuation processes determine the ultimate limits of spatial resolution. Today’s advanced NEMS devices are capable of resolving molecular-scale analytes. One of the most exciting current fields of application for this method focuses on the analysis of large proteins and biomolecular complexes – for example, membrane proteins, antibody isoforms, organelles, and viruses – in their native (unfragmented and non-denatured) state.

[1] Naik, A. K., Hanay, M. S., Hiebert, W. K., Feng, X. L. & Roukes, M. L., Towards Single-molecule Nanomechanical Mass Spectrometry. Nature Nanotechnology 4, 445–450 (2009).
[2] Hanay, M. S., Kelber, S. I., Naik, A. K., Chi, D., Hentz, S., Bullard, E. C., Colinet, E., Duraffoug, L. & Roukes, M. L., Single-protein Nanomechanical Mass Spectrometry in Real Time. Nature Nanotechnology, 7, 602-608 (2012).
[3] Hanay, M. S., Kelber, S. I., O'Connell, C. D., Mulvaney, P., Sader, J. E. & Roukes, M. L., Inertial Imaging with Nanomechanical Systems. Nature Nanotechnology 10, 339-344 (2015).

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