Our work focuses on dynamic properties of molecules, notably bio-macromolecules, using NMR or ESR probes as reporters. The probe is a (typically small) structural moiety housing an NMR nucleus or an unpaired electron. In the last fifteen years we developed the slowly relaxing local structure (SRLS) approach for the analysis of NMR relaxation in proteins in aqueous solution.
Unlike other methods in the field, SRLS (1) relies on tensorial representation of the relevant physical quantities, (2) accounts for dynamical coupling between the overall tumbling of the protein and the local motion of the (physically attached) probe. The former feature, which is always important, renders SRLS general. The latter feature is important when the time scale separation between the overall reorientation of the protein and the local motion of the probe is not large.
The limit of SRLS in which the protein is “frozen”, called the “microscopic order macroscopic disorder” (MOMD) approach, is treating internally mobile polycrystalline proteins. In the last couple of years we applied MOMD to protein dynamics by NMR in the solid-state.
Excerpts of publications authored by Eva Meirovitch can be found at: