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)


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)


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)


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)


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)


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)


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)


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)


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)


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)


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)


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)