@article{tesch_pourmoazzen_awosanya_nevzorov_2018, title={Uniaxial Diffusional Narrowing of NMR Lineshapes for Membrane Proteins Reconstituted in Magnetically Aligned Bicelles and Macrodiscs}, volume={49}, ISSN={["1613-7507"]}, DOI={10.1007/s00723-018-1056-4}, number={12}, journal={APPLIED MAGNETIC RESONANCE}, author={Tesch, Deanna M. and Pourmoazzen, Zhaleh and Awosanya, Emmanuel O. and Nevzorov, Alexander A.}, year={2018}, month={Dec}, pages={1335–1353} }
 @article{koroloff_tesch_awosanya_nevzorov_2017, title={Sensitivity enhancement for membrane proteins reconstituted in parallel and perpendicular oriented bicelles obtained by using repetitive cross-polarization and membrane-incorporated free radicals}, volume={67}, ISSN={["1573-5001"]}, DOI={10.1007/s10858-017-0090-0}, abstractNote={Multidimensional separated local-field and spin-exchange experiments employed by oriented-sample solid-state NMR are essential for structure determination and spectroscopic assignment of membrane proteins reconstituted in macroscopically aligned lipid bilayers. However, these experiments typically require a large number of scans in order to establish interspin correlations. Here we have shown that a combination of optimized repetitive cross polarization (REP-CP) and membrane-embedded free radicals allows one to enhance the signal-to-noise ratio by factors 2.4-3.0 in the case of Pf1 coat protein reconstituted in magnetically aligned bicelles with their normals being either parallel or perpendicular to the main magnetic field. Notably, spectral resolution is not affected at the 2:1 radical-to-protein ratio. Spectroscopic assignment of Pf1 coat protein in the parallel bicelles has been established as an illustration of the method. The proposed methodology will advance applications of oriented-sample NMR technique when applied to samples containing smaller quantities of proteins and three-dimensional experiments.}, number={2}, journal={JOURNAL OF BIOMOLECULAR NMR}, author={Koroloff, Sophie N. and Tesch, Deanna M. and Awosanya, Emmanuel O. and Nevzorov, Alexander A.}, year={2017}, month={Feb}, pages={135–144} }
 @article{tesch_nevzorov_2014, title={Sensitivity enhancement and contrasting information provided by free radicals in oriented-sample NMR of bicelle-reconstituted membrane proteins}, volume={239}, ISSN={["1096-0856"]}, DOI={10.1016/j.jmr.2013.11.010}, abstractNote={Elucidating structure and topology of membrane proteins (MPs) is essential for unveiling functionality of these important biological constituents. Oriented-sample solid-state NMR (OS-NMR) is capable of providing such information on MPs under nearly physiological conditions. However, two dimensional OS-NMR experiments can take several days to complete due to long longitudinal relaxation times combined with the large number of scans to achieve sufficient signal sensitivity in biological samples. Here, free radicals 5-DOXYL stearic acid, TEMPOL, and CAT-1 were added to uniformly 15N-labeled Pf1 coat protein reconstituted in DMPC/DHPC bicelles, and their effect on the longitudinal relaxation times (T1Z) was investigated. The dramatically shortened T1Z’s allowed for the signal gain per unit time to be used for either: (i) up to a threefold reduction of the total experimental time at 99% magnetization recovery or (ii) obtaining up to 74% signal enhancement between the control and radical samples during constant experimental time at “optimal” relaxation delays. In addition, through OS-NMR and high-field EPR studies, free radicals were able to provide positional constraints in the bicelle system, which provide a description of the location of each residue in Pf1 coat protein within the bicellar membranes. This information can be useful in the determination of oligomerization states and immersion depths of larger membrane proteins.}, journal={JOURNAL OF MAGNETIC RESONANCE}, author={Tesch, Deanna M. and Nevzorov, Alexander A.}, year={2014}, month={Feb}, pages={9–15} }