Magnetic Resonance




Assoc. Prof.



Life Sciences Building 212, 4th Floor

Career Highlights:

Research Interests and Goals:

        In general, our research goal is to characterize the motional state of proteins, peptides, and other biological macromolecules to help answer questions of biological interest. Globular proteins constitute an essential component of living organisms and perform a wide range of functions such as catalysis, electron transport, enhancing the rate of DNA transcription, etc. These activities unfold Ch solution, where mobility is crucial for the adaptation of structures to particular functions. NMR is the only currently available physical method that can probe motional aspects at the atom level over a very large timescale, and provide elaborate information.

Previous and Current Research:

        Various experimental and theoretical aspects of molecular structure and mobility in liquids, solid, and liquid crystalline phases studied by Magnetic Resonance methods.

        The dynamic structure of biological macromolecules studied by multidimensional heteronuclear NMR techniques and relationship to biological function.

Future Projects:

        Extension of current work, and development of new methodologies for extracting information on the mobility of biological macromolecules, and its relationship to structure and function.

Present Research Group

  • Prof. Yury E. Shapiro, Ph.D. Visiting Scientist
  • Rachel Rosenthal, M.Sc. Ph.D. student
  • Selected Publications

    1. Meirovitch, E. Distinctive properties of tubular solar chemical reactors. J. of Solar Energy Engineering, 113, 188 (1991).
    2. Diver, R.B, Fish, J.D., Levitan, R., Levy, M., Meirovitch, E., Rosin, H., Paripatyadar, S.A. and Richardson, J.T. Solar test of an integrated sodium reflux heat pipe receiver/reactor for thermochemical energy transport. Solar Energy, 113, 48, 21 (1992).
    3. Levy, M., Levitan, R., Meirovitch, E., Segal, A., Rosin, H. and Rubin, R. Chemical reactions in a solar furnace. 2. Direct heating of a vertical reactor in an insulated receiver; experiments and computer simulation. Solar Energy, 113, 48, 395 (1992).
    4. Meirovitch, H., Meirovitch, E., Michel, A.G. and Vásquez, M. A simple and effective procedure for conformational search of macromolecules: Application to Met- and Leu-enkephalin. J. Phys. Chem., 98, 6241 (1994).
    5. Vásquez, M., Meirovitch, E. and Meirovitch, H. A free energy based Monte Carlo minimization procedure for biomolecules. J. Phys. Chem., 98, 9383 (1994).
    6. Meirovitch, H., Meirovitch, E. and Lee, J. New theoretical methodology for elucidating the solution structure of peptides from NMR data. I. The relative contribution of low energy microstates to the partition function. J. Phys. Chem. 99, 4847 (1995).
    7. Meirovitch, E. and Meirovitch, H. New theoretical methodology for elucidating the solution structure of peptides from NMR data. II. Free energy of dominant microstates of leu-enkephalin and population-weighted average NOE intensities. Biopolymers, 38, 69 (1996).
    8. Meirovitch, H. and Meirovitch, E. New theoretical methodology for elucidating the solution structure of peptides from NMR data. III. Solvation effects. J. Phys. Chem., 10, 5123 (1996).
    9. Meirovitch, H. Meirovitch, E. and Vásquez, M. The efficiency of Monte Carlo minimization procedures for locating low free energy states of peptides. J. Comput. Chem. 18, 240-253 (1997).
    10. Meirovitch, E., Sinev, M.A. and Sineva, E.V. Sequence-specific 1H, 15N and 13C assignment of adenylate kinase from Escherichia coli in complex with the inhibitor AP5A. J. Bimol. NMR, 13, 195 (1999).