Prof. Eva Meirovitch is a physical chemist, and a full professor in the Mina and Everard Goodman Faculty of Life Sciences. Her field of expertise is Nuclear Magnetic Resonance (NMR), in particular the elucidation of dynamic and structural properties of molecules using NMR spin relaxation methods.
Globular proteins constitute an essential component of living organisms and perform a wide range of functions including catalysis, electron transport, and enhancing the rate of DNA transcription. Protein mobility is crucial for the adaptation of structures to their specific functions.
NMR spin relaxation is a powerful physical method that can investigate motional aspects at the atomic level over a very large timescale.
Prof. Meirovitch and her team are involved in the development of stochastic models for the analysis of experimental NMR relaxation data in terms of the nature of the global and local motions in proteins and other bio-macromolecules.
The dynamic NMR probes are typically chemical bonds comprised by virtually every amino-acid in the protein.
Hence, one can map out the protein structure extensively, providing ample information on its internal mobility. In particular, NMR spin relaxation provides information of motional rates, local geometry, and the local potentials that restrict the internal motion of the NMR probe.
Protein flexibility is complex. The thrust of the research in the group of Prof. Meirovitch is to develop theoretical models that are realistic and physically sound, are tractable computationally, and match the sensitivity of the experimental data. The traditional Model-Free (MF) approach for translating NMR spin relaxation data into a dynamic picture is over-simplified. Consequently, a physically vague picture of protein dynamics emerges.
Meirovitch’s team has been involved in development of the Slowly Relaxing Local Structure (SRLS) approach for NMR spin relaxation in proteins. SRLS may be considered the generalization of MF yielding the latter in simple limits. Work carried out in the last 10 years has shown the SRLS provides a significantly more insighful and accurate picture of protein dynamics than MF.
The SRLS approach has been applied so far to the amide bond as reporter of protein backbone dynamics, and the methyl group as reporter of side-chain dynamics. Application to additional probes is contemplated. Likewise, application to different types of experiments (mainly cross-correlated relaxation) will be pursued. SRLS is also uniquely suited to analyze consistently and coherently residual dipolar couplings, which emerge when the protein is dissolved in anisotropic solvents.
This development is in progress. The current implementation of SRLS will be enhanced along lines found to be important by work carried out so far. Increased efficiency of the computer programs, that will render SRLS a user-friendly generally applicable theoretical/computational tool to be used by the NMR community, is among future objectives.