Publications
2023
32. Bichitra, B.; Acharya, G.R.; Grajeda, D.; Emersono, M.S; Harris, M.A.; Abeykoon, AM.M.; Sangoro, J.; Baker, G.A.; Nieuwkoop, A.J.; Margulis, C.J.; Do Ionic Liquids Slow Down in Stages?, J. Am. Chem. Soc. 2023, (https://doi.org/10.1021/jacs.3c08639)
31. Osborn Popp, T.M.; Matchett, B.T.; Green, R.G. Chhabra, I.; Mumudi, S.; Bernstein, A.D.; Perodeau, J.R.; Nieuwkoop, A.J.; 3D-Printable centrifugal devices for biomolecular solid state NMR rotors, J. Mag. Res. 2023, 354, 107524. (https://doi.org/10.1016/j.jmr.2023.107524)
30. Ogbodo, R.; Karunarate, W.V.; Acharya, G.R.; Emerson, M.S.; Mughal, M.; Yuen, H.M.; Zmich, N.; Nembhard S.; Furong, W.; Shirota, H.; Lall-Ramnarine, L.; Castner Jr.; E.W.; Wishart, J.; Nieuwkoop, A.J.; Margulis, C.J.; Structural origins of viscosity in imidazolium and pyrrolidinium ionic liquids coupled with the NTf2– anion, J. Chem. B. 2023, 127(28), 6342-6353. (https://doi.org/10.1021/acs.jpcb.3c02604)
29. Perodeau, J.; Arbogast, L.W; Nieuwkoop A.J.; Solid-State NMR characterization of Lyopholized formulations of monoclonal antibody therapeutics, Mol. Phamaceutics. 2023, 20(3), 1480-1489. (https://doi.org/10.1021/acs.molpharmaceut.2c00676)
28. Zhang G.; Xie F.; Osborn Popp T.M.; Patel A.; Cedeño Morales E.M.; Tan K.; Crichton R.; Hall G.; Zhang, J.; Nieuwkoop A.J.; Li J.; A series of cation-modified robust zirconium-based metal-organic frameworks for carbon dioxide capture, CrystEngComm. 2023, 25(7), 1067-1075. (https://doi.org/10.1039/D2CE01633H)
2022
27. Yang, Y.; Distaffen, H.; Jalali, S.; Nieuwkoop, A.J.; Nilsson, B.L.; C.L.; Atomic insights into Amyloid-Induced membrane damage. ACS Chem Neurosci. 2022, 13(18), 2766-2777. (https://doi.org/10.1021/acschemneuro.2c00446)
2021
26. Palmere, R.D.; Case, D.A.; Nieuwkoop, A.J; Simulations of Kindlin-2 PIP binding domains reveal protonation-dependent membrane binding modes. Biophys J. 2021, 120 (24), 5504-5512. (https://doi.org/10.1016/j.bpj.2021.11.021)
25. Miles, C.E.; Bernstein, A.D.; Osborn Popp, T.M.; Murthy, N.S.; Nieuwkoop, A.J; Gormley, A.J.; Control of Drug Release from Microparticles by Tuning Their Crystalline Textures: A Structure-Activity Study. ACS Appl. Polym. Mater. 2021, 3 (12) 6548-6561. (https://doi.org/10.1021/acsapm.1c01254)
24. Velasco, E.; Xian, S.; Teat, S.J.; Olson, D.H.; Tan, K.; Ullah, S.; Osborn Popp, T.M.; Bernstein, A.D.; Okekan, K.A.;Nieuwkoop, A. J.; Thornhauser, T.; Li, J.; Flexible Zn-MOF with Rare Underlying scu Topology for Effective Separation of C6 Alkane Isomers. ACS Appl.Mater. Interfaces 2021, 13 (44) 51997-52005. (https://doi.org/10.1021/acsami.1c08678)
2020
23. Friedrich, D.; Perodeau, J.; Nieuwkoop, A. J.; Oschkinat, H., MAS NMR detection of hydrogen bonds for protein secondary structure characterization. Biomol. NMR 2020, 74 (4-5), 247-256. (http://doi.org/10.1007/s10858-020-00307-z)
22. Friedrich, D.; Brunig, F. N.; Nieuwkoop, A. J.; Netz, R. R.; Hegemann, P.; Oschkinat, H., Collective exchange processes reveal an active site proton cage in bacteriorhodopsin. Commun Biol 2020, 3 (1), 4. (http://doi.org/10.1038/s42003-019-0733-7)
21. Hernando, M.; Orriss, G.; Perodeau, J.; Lei, S.; Ferens, F. G.; Patel, T. R.; Stetefeld, J.; Nieuwkoop, A. J.; O’Neil, J. D., Solution structure and oligomeric state of the E. coliglycerol facilitator. Biophys. Acta, Biomembr. 2020, 1862 (5), 183191. (http://doi.org/10.1016/j.bbamem.2020.183191)
2017
20. Retel, J. S., Nieuwkoop, A. J., Hiller, M., Higman, V. A., Barbet-Massin, E., Stanek, J., Andreas, L. B., Franks, W. T., van Rossum, B. J., Vinothkumar, K. R., Handel, L., de Palma, G. G., Bardiaux, B., Pintacuda, G., Emsley, L., Kühlbrandt, W., Oschkinat, Hartmut “Structure of Outer Membrane Protein G in Lipid Bilayers” Nat. Comm. 2017 8(1), 2073-2083. (http://doi.org/10.1038/s41467-017-02228-2)
2016
19. Tuttle, M. D., Comellas, G., Nieuwkoop, A. J., Covell, D. J., Berthold, D. A., Kloepper, K. D., Courtney, J. M., Kim, J. K., Barclay, A. M., Kendall, A., Wan, W., Stubbs, G., Schwieters, C. D., Lee, V. M. Y., George, J. M. and Rienstra, C. M. “Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein” Nat. Struct. Mol. Biol. 2016 23(5), 409-15. (http://doi.org/10.1038/nsmb.3194)
2015
18. Nieuwkoop, A. J., Franks, W. T., Rehbein, K., Diehl, A., Akbey, U., Engelke, F., Emsley, L., Pintacuda, G. and Oschkinat, H. “Sensitivity and resolution of proton detected spectra of a deuterated protein at 40 and 60 kHz magic-angle-spinning” J. Biomol. NMR. 2015 61(2), 161-71. (http://doi.org/10.1007/s10858-015-9904-0)
2014
17. Barbet-Massin, E., Pell, A. J., Retel, J. S., Andreas, L. B., Jaudzems, K., Franks, W. T., Nieuwkoop, A. J., Hiller, M., Higman, V., Guerry, P., Bertarello, A., Knight, M. J., Felletti, M., Le Marchand, T., Kotelovica, S., Akopjana, I., Tars, K., Stoppini, M., Bellotti, V., Bolognesi, M., Ricagno, S., Chou, J. J., Griffin, R. G., Oschkinat, H., Lesage, A., Emsley, L., Herrmann, T. and Pintacuda, G. “Rapid proton-detected NMR assignment for proteins with fast magic angle spinning” J. Am. Chem. Soc. 2014 136(35), 12489-97. (http://doi.org/10.1021/ja507382j)
16. Anderson, T. M., Clay, M. C., Cioffi, A. G., Diaz, K. A., Hisao, G. S., Tuttle, M. D., Nieuwkoop, A. J., Comellas, G., Maryum, N., Wang, S., Uno, B. E., Wildeman, E. L., Gonen, T., Rienstra, C. M. and Burke, M. D. “Amphotericin forms an extramembranous and fungicidal sterol sponge” Nat. Chem. Biol. 2014 10(5), 400-6. (http://doi.org/10.1038/nchembio.1496)
15. Akbey, U., Nieuwkoop, A. J., Wegner, S., Voreck, A., Kunert, B., Bandara, P., Engelke, F., Nielsen, N. C. and Oschkinat, H. “Quadruple-resonance magic-angle spinning NMR spectroscopy of deuterated solid proteins” Angew Chem Int Ed Engl. 2014 53(9), 2438-42. (http://doi.org/10.1002/anie.201308927)
2012
14. Zhou, D. H., Nieuwkoop, A. J., Berthold, D. A., Comellas, G., Sperling, L. J., Tang, M., Shah, G. J., Brea, E. J., Lemkau, L. R. and Rienstra, C. M. “Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy” J. Biomol. NMR. 2012 54(3), 291-305. (http://doi.org/10.1007/s10858-012-9672-z)
2011
13. Wylie, B. J., Sperling, L. J., Nieuwkoop, A. J., Franks, W. T., Oldfield, E. and Rienstra, C. M. “Ultrahigh resolution protein structures using NMR chemical shift tensors” Proc. Natl. Acad. Sci. U. S. A. 2011 108(41), 16974-9. (http://doi.org/10.1073/pnas.1103728108)
12. Tang, M., Sperling, L. J., Berthold, D. A., Schwieters, C. D., Nesbitt, A. E., Nieuwkoop, A. J., Gennis, R. B. and Rienstra, C. M. “High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data” J. Biomol. NMR. 2011 51(3), 227-33. (http://doi.org/10.1007/s10858-011-9565-6)
11. Comellas, G., Lopez, J. J., Nieuwkoop, A. J., Lemkau, L. R. and Rienstra, C. M. “Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR” J Magn Reson. 2011 209(2), 131-5. (http://doi.org/10.1016/j.jmr.2010.12.011)
10. Comellas, G., Lemkau, L. R., Nieuwkoop, A. J., Kloepper, K. D., Ladror, D. T., Ebisu, R., Woods, W. S., Lipton, A. S., George, J. M. and Rienstra, C. M. “Structured regions of alpha-synuclein fibrils include the early-onset Parkinson’s disease mutation sites” J. Mol. Biol. 2011 411(4), 881-95. (http://doi.org/10.1016/j.jmb.2011.06.026)
9. Boettcher, J. M., Davis-Harrison, R. L., Clay, M. C., Nieuwkoop, A. J., Ohkubo, Y. Z., Tajkhorshid, E., Morrissey, J. H. and Rienstra, C. M. “Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers” Biochemistry. 2011 50(12), 2264-73. (http://doi.org/10.1021/bi1013694)
2010
8. Sperling, L. J., Nieuwkoop, A. J., Lipton, A. S., Berthold, D. A. and Rienstra, C. M. “High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field” J. Biomol. NMR. 2010 46(2), 149-55. (http://doi.org/10.1007/s10858-009-9389-9)
7. Nieuwkoop, A. J. and Rienstra, C. M. “Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy” J. Am. Chem. Soc. 2010 132(22), 7570-1. (http://doi.org/10.1021/ja100992y)
6. Nielsen, A. B., Straaso, L. A., Nieuwkoop, A. J., Rienstra, C. M., Bjerring, M. and Nielsen, N. C. “Broadband Heteronuclear Solid-State NMR Experiments by Exponentially Modulated Dipolar Recoupling without Decoupling” J. Phys. Chem. Lett. 2010 1(13), 1952-6. (http://doi.org/10.1021/jz100564j)
5. Kijac, A., Shih, A. Y., Nieuwkoop, A. J., Schulten, K., Sligar, S. G. and Rienstra, C. M. “Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance” Biochemistry. 2010 49(43), 9190-8. (http://doi.org/10.1021/bi1013722)
2009
4. Nieuwkoop, A. J., Wylie, B. J., Franks, W. T., Shah, G. J. and Rienstra, C. M. “Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy” J. Chem. Phys. 2009 131(9), 095101. (http://doi.org/10.1063/1.3211103)
2008
3. Franks, W. T., Wylie, B. J., Schmidt, H. L., Nieuwkoop, A. J., Mayrhofer, R. M., Shah, G. J., Graesser, D. T. and Rienstra, C. M. “Dipole tensor-based atomic-resolution structure determination of a nanocrystalline protein by solid-state NMR” Proc. Natl. Acad. Sci. U. S. A. 2008 105(12), 4621-6. (http://doi.org/10.1073/pnas.0712393105)
2007
2. Zhou, D. H., Shea, J. J., Nieuwkoop, A. J., Franks, W. T., Wylie, B. J., Mullen, C., Sandoz, D. and Rienstra, C. M. “Solid-state protein-structure determination with proton-detected triple-resonance 3D magic-angle-spinning NMR spectroscopy” Angew Chem Int Ed Engl. 2007 46(44), 8380-3. (http://doi.org/10.1002/anie.200702905)
1. Graesser, D. T., Wylie, B. J., Nieuwkoop, A. J., Franks, W. T. and Rienstra, C. M. “Long-range 19F-15N distance measurements in highly-13C, 15N-enriched solid proteins with 19F-dephased REDOR shift (FRESH) spectroscopy” Magn. Reson. Chem. 2007 45 Suppl 1(S129-34. (http://doi.org/10.1002/mrc.2126)