Martin Lab Research

The focus of our research is the development and application of solid-state NMR methods for proteins that are  neither crystalline nor soluble in their biologically relevant states. or example, many physiologically important proteins are associated with phospholipid membranes. The structure and function of these proteins may depend on interactions with the lipid environment and may not remain intact when the protein is removed from the membrane. Other locally ordered protein networks are implicated in disease states, such as amyloid fibrils or the branched filaments found in cataracts of the eye lens. Because they are typically insoluble and non-crystalline, these materials are not amenable to structure determination by traditional biophysical techniques such as solution-state NMR or single-crystal X-ray diffraction. They may also have complicated intermolecular interactions that are not easily probed by single-molecule studies. Therefore, locally ordered protein networks represent a frontier of structural biology.

Solid-state NMR is particularly amenable to the investigation of these samples because of its ability to directly probe internuclear interactions and its requirement for only local order.   We are developing advanced NMR methodologies that will yield correlations between isotropic spectra allowing unambiguous assignment of the signals from each nucleus with detailed distance or orientational measurements.    Aspects of this research include instrumentation design and construction,  implementation of new pulse sequences, and optimization of  sample preparation.