Dr. John J. Kasianowicz

CV

Education

Science management courses (2003) MIT Sloan Management School, Boston, MA

Ph.D. (1987) Physiology & Biophysics, SUNY at Stony Brook, Stony Brook, NY.

M.A. (1981) Physics, SUNY at Stony Brook, Stony Brook, NY

B.A. (1979) Physics, Boston University, Boston, MA (with Distinction)

Publikationen (Auswahl)

• Kasianowicz, J.J., E. Brandin, D. Branton, and D.W. Deamer. 1996. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. (USA) 93, 13770-13773.
• Kasianowicz, J.J., J.W.F. Robertson, E.R. Chan, J.E. Reiner, and V.M. Stanford. 2008. Nanoscopic porous sensors.  Annual Reviews of Analytical Chemistry 1, 737-766.
• Robertson, J.W.F., C.G. Rodrigues, V.M. Stanford, K. Rubinson, O.V. Krasilnikov, and J.J. Kasianowicz. 2007. Single molecule mass spectrometry in solution using solitary nanopores.  Proc. Natl. Acad. Sci. (USA) 104, 8207-8211.
• Reiner, J.E., J.W.F. Robertson, D.L. Burden, L.K. Burden, A. Balijepalli, and J.J. Kasianowicz.  2013.  Temperature sculpting in yoctoliter volumes.  J. Am. Chem. Soc. 135, 3087-3094.
• Kasianowicz, J.J. and S.M. Bezrukov. 1995. Protonation dynamics of the a-toxin ion channel from spectral analysis of pH dependent current fluctuations.  Biophysical J. 69, 94-105.

FRIAS-Projekt

Identification of proteins using single nanometer-scale pores

Based on earlier work by my group (Kasianowicz 1995, Bezrukov 1996, Kasianowicz 2012) nanometer-scale pores are now used for detecting and physically characterizing nucleic acids, ions, and synthetic polymers (Kasianowicz 2008, Muthukumar 2016).  The method, which has become popular in research laboratories worldwide, is now simple:  when a molecule enters an ion channel, it can interact with the pore wall long enough to cause a temporary reduction in the ionic current.  The ability to accurately measure both the current changes and residence times of the molecules in the pore ultimately led to two different methods for sequencing DNA (Kasianowicz 1996, Derrington 2010, Kumar 2012, Fuller 2016), a new technique to discriminate between different length polymers (Robertson 2007), and a novel way to measure how DNA processivity enzymes work (Derrington 2015).  We propose to identify proteins of interest by first cleaving them with proteases and then driving the resultant polypeptide fragments into the pore for analysis.  Because many proteases act at specific sites in proteins, and the primary sequences of different proteins are dissimilar, the voltage- and protease-dependent patterns of the current blockades and residence times of the fragments in the pore should provide a unique fingerprint to identify proteins of interest.