{"id":591,"date":"2023-06-17T20:48:26","date_gmt":"2023-06-17T20:48:26","guid":{"rendered":"https:\/\/sites.rutgers.edu\/nieuwkoop-lab\/?page_id=591"},"modified":"2025-12-11T21:29:47","modified_gmt":"2025-12-11T21:29:47","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.rutgers.edu\/nieuwkoop-lab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

2025<\/strong><\/p>\n

37. Ogbodo, R.; Ansar, I.; Adu, C.;<\/strong> Lall-Ramnarine, S.I.; Wishart, J.F.; Nieuwkoop, A.J.; <\/strong>Margulis, C.J.; Tethered from the head and from the tail; the structure of hydroxyl-functionalized ionic liquids J. Phys. Chem. Lett.<\/em>\u00a0<\/i><\/em>\u00a02025<\/strong>, 16 (12982-12988) (https:\/\/doi.org\/10.1021\/acs.jpclett.5c03046<\/a>)<\/span><\/p>\n

36. Mustapha, Z.O.; Ozturk, E.H.; Lefkin, B.E.; Grajeda, D.;\u00a0Nieuwkoop, A.J.; <\/strong>Measuring long-range contacts in a fully protonated protein at 105 kHz magic angle spinning \u00a0Biomol. NMR. <\/i><\/em>\u00a02025<\/strong>,\u00a0 79 (331-339) (https:\/\/doi.org\/10.1007\/s10858-025-00477-8)<\/a><\/span><\/p>\n

35. Ogbodo, R.; Acharya, G.R.;<\/strong> Yuen, H.M.; Zmich, N.; Wang, F.; Shirota, H.; Lall-Ramnarine, S.I.; Wishart, J.F.;\u00a0 Nieuwkoop, A.J.; <\/strong>Margulis, C.J.; Structure of novel phosphonium-based ionic liquids with S and O substitutions from experiments and a mixed quantum-classical approach, \u00a0J. Phys. Chem.<\/em> B.<\/em> 2025<\/strong>, 129 (14) 3691-3701 (https:\/\/doi.org\/10.1021\/acs.jpcb.5c001297)<\/a><\/span><\/p>\n

34.\u00a0Osborn Popp, T.M.;\u00a0 <\/strong>Karthikeyan, M.; Herman, E.M.;\u00a0 Dufur, A.C.; Vetriani, C.; \u00a0Nieuwkoop, A.J.; <\/strong>Measurement of phospholipid lateral diffusion at high pressure by in situ magic-angle spinning NMR spectroscopy, \u00a0Commun. Chem<\/em>. 2025<\/strong>, 8 (49) (https:\/\/doi.org\/10.1038\/s42004-025-01449-7)<\/a><\/span><\/p>\n

2024<\/strong><\/p>\n

33. Bernstein, A.D.<\/strong>;\u00a0Asante, Ampadu, G.A.; Yang, Y.; Acharya, G.R.; Osborn Popp, T.M.; Nieuwkoop, A.J.;\u00a0<\/strong>Effects of Ca2+<\/sup> on the structure and dynamics of PIP3 <\/sub>in model membranes containing PC and PS, Biochem<\/em>. 2024<\/strong>, 64(1) 127-137 (https:\/\/doi.org\/10.1021\/acs.biochem.4c00513<\/a>)<\/span><\/p>\n

2023<\/strong><\/p>\n

32. Bichitra, B.; Acharya, G.R.<\/strong>; Grajeda, D.<\/strong>; Emersono, M.S; Harris, M.A.; Abeykoon, AM.M.; Sangoro, J.; Baker, G.A.; Nieuwkoop, A.J.<\/strong>; Margulis, C.J.; Do Ionic Liquids Slow Down in Stages?, J. Am. Chem. Soc. 2023<\/strong>,\u00a0 145 (47), 25518-25522 (https:\/\/doi.org\/10.1021\/jacs.3c08639<\/a>)<\/p>\n

31. Osborn Popp, T.M<\/strong>.; Matchett, B.T.<\/strong>; Green, R.G.;<\/strong>\u00a0Chhabra, I.<\/strong>; Mumudi, S.<\/strong>; Bernstein, A.D.<\/strong>; Perodeau, J.R.<\/strong>; Nieuwkoop, A.J.<\/strong>; 3D-Printable centrifugal devices for biomolecular solid state NMR rotors,\u00a0J. Mag. Res.\u00a02023,\u00a0<\/strong><\/em>354, 107524. (https:\/\/doi.org\/10.1016\/j.jmr.2023.107524<\/a>)<\/p>\n

30. Ogbodo, R.; Karunarate, W.V.; Acharya, G.R.; <\/strong>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.;<\/strong> Margulis, C.J.; Structural origins of viscosity in imidazolium and pyrrolidinium ionic liquids coupled with the NTf2<\/sub>\u2013\u00a0<\/sup><\/span> anion,\u00a0J. Chem. B. <\/em>2023, <\/strong>127(28), 6342-6353. (https:\/\/doi.org\/10.1021\/acs.jpcb.3c02604<\/a>)<\/p>\n

29. Perodeau<\/strong>, J.; Arbogast, L.W; Nieuwkoop A.J.;<\/strong> Solid-State NMR characterization of Lyopholized formulations of monoclonal antibody therapeutics, Mol. Phamaceutics<\/em>. 2023<\/strong>, 20(3), 1480-1489. (https:\/\/doi.org\/10.1021\/acs.molpharmaceut.2c00676<\/a>)<\/p>\n

28. Zhang G.; Xie F.; Osborn Popp T.M.;<\/strong>\u00a0Patel A.; Cede\u00f1o Morales E.M.; Tan K.; Crichton R.; Hall G.; Zhang, J.; Nieuwkoop A.J.;<\/strong> Li J.; A series of cation-modified robust zirconium-based metal-organic frameworks for carbon dioxide capture, CrystEngComm<\/em>. 2023<\/strong>, 25(7), 1067-1075. (https:\/\/doi.org\/10.1039\/D2CE01633H<\/a>)<\/p>\n

2022<\/strong><\/p>\n

27. Yang<\/strong>, Y.; <\/strong>Distaffen, H.; Jalali, S.; Nieuwkoop, A.J.;<\/strong> Nilsson, B.L.; C.L.; Atomic insights into Amyloid-Induced membrane damage. ACS Chem Neurosci.<\/em> 2022<\/strong>, 13(18), 2766-2777. (https:\/\/doi.org\/10.1021\/acschemneuro.2c00446<\/a>)<\/p>\n

2021<\/strong><\/p>\n

26.\u00a0Palmere, R.D.;<\/strong>\u00a0Case, D.A.;\u00a0Nieuwkoop, A.J;<\/strong>\u00a0Simulations of Kindlin-2 PIP binding domains reveal protonation-dependent membrane binding modes.\u00a0Biophys J.<\/i><\/em>\u00a02021,<\/strong>\u00a0120<\/i><\/em>\u00a0(24), 5504-5512. (https:\/\/doi.org\/10.1016\/j.bpj.2021.11.021<\/a>)<\/p>\n

25. Miles, C.E.;\u00a0Bernstein, A.D.; Osborn Popp, T.M.;<\/strong>\u00a0Murthy, N.S.;\u00a0Nieuwkoop, A.J;\u00a0<\/strong>Gormley, A.J.; Control of Drug Release from Microparticles by Tuning Their Crystalline Textures: A Structure-Activity Study.\u00a0ACS Appl. Polym. Mater.<\/i><\/em>\u00a02021,<\/strong>\u00a03<\/i><\/em>\u00a0(12) 6548-6561. (https:\/\/doi.org\/10.1021\/acsapm.1c01254<\/a>)<\/p>\n

24.\u00a0Velasco, E.; Xian, S.; Teat, S.J.; Olson, D.H.; Tan, K.; Ullah, S.;\u00a0Osborn Popp, T.M.; Bernstein, A.D.<\/strong>; Okekan, K.A.;Nieuwkoop, A. J.<\/strong>; Thornhauser, T.; Li, J.; Flexible Zn-MOF with Rare Underlying scu Topology for Effective Separation of C6 Alkane Isomers.\u00a0ACS Appl.Mater. Interfaces\u00a0<\/i><\/em>2021,<\/strong>\u00a013<\/i><\/em>\u00a0(44) 51997-52005. (https:\/\/doi.org\/10.1021\/acsami.1c08678<\/a>)<\/p>\n

2020<\/strong><\/p>\n

23.\u00a0Friedrich, D.;\u00a0Perodeau, J.<\/strong>;\u00a0Nieuwkoop, A. J.<\/strong>; Oschkinat, H., MAS NMR detection of hydrogen bonds for protein secondary structure characterization.\u00a0Biomol. NMR. <\/i><\/em>2020,<\/strong>\u00a074<\/i><\/em>\u00a0(4-5), 247-256. (http:\/\/doi.org\/10.1007\/s10858-020-00307-z<\/a>)<\/p>\n

22.\u00a0 Friedrich, D.; Brunig, F. N.;\u00a0Nieuwkoop, A. J.<\/strong>; Netz, R. R.; Hegemann, P.; Oschkinat, H., Collective exchange processes reveal an active site proton cage in bacteriorhodopsin.\u00a0Commun Biol\u00a0<\/i><\/em>2020,<\/strong>\u00a03<\/i><\/em>\u00a0(1), 4. (http:\/\/doi.org\/10.1038\/s42003-019-0733-7<\/a>)<\/p>\n

21.\u00a0 Hernando, M.; Orriss, G.;\u00a0Perodeau, J.<\/strong>; Lei, S.; Ferens, F. G.; Patel, T. R.; Stetefeld, J.;\u00a0Nieuwkoop, A. J.<\/strong>; O’Neil, J. D., Solution structure and oligomeric state of the E. coliglycerol facilitator.\u00a0Biophys. Acta, Biomembr.\u00a0<\/i><\/em>2020,<\/strong>\u00a01862<\/i><\/em>\u00a0(5), 183191. (http:\/\/doi.org\/10.1016\/j.bbamem.2020.183191<\/a>)<\/p>\n

2017<\/strong><\/p>\n

20.\u00a0\u00a0 Retel, J. S.,\u00a0Nieuwkoop, A. J.<\/strong>, 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., K\u00fchlbrandt, W., Oschkinat, Hartmut “Structure of Outer Membrane Protein G in Lipid Bilayers”\u00a0Nat. Comm.\u00a02017<\/strong>\u00a08(1), 2073-2083. (http:\/\/doi.org\/10.1038\/s41467-017-02228-2<\/a>)<\/p>\n

2016<\/strong><\/p>\n

19.\u00a0\u00a0 Tuttle, M. D., Comellas, G.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02016<\/strong>\u00a023(5), 409-15. (http:\/\/doi.org\/10.1038\/nsmb.3194<\/a>)<\/p>\n

2015<\/strong><\/p>\n

18. \u00a0\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02015<\/strong>\u00a061(2), 161-71. (http:\/\/doi.org\/10.1007\/s10858-015-9904-0<\/a>)<\/p>\n

2014<\/strong><\/p>\n

17. \u00a0 Barbet-Massin, E., Pell, A. J., Retel, J. S., Andreas, L. B., Jaudzems, K., Franks, W. T.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02014<\/strong>\u00a0136(35), 12489-97. (http:\/\/doi.org\/10.1021\/ja507382j<\/a>)<\/p>\n

16. \u00a0 Anderson, T. M., Clay, M. C., Cioffi, A. G., Diaz, K. A., Hisao, G. S., Tuttle, M. D.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02014<\/strong>\u00a010(5), 400-6. (http:\/\/doi.org\/10.1038\/nchembio.1496<\/a>)<\/p>\n

15.\u00a0 Akbey, U.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02014<\/strong>\u00a053(9), 2438-42. (http:\/\/doi.org\/10.1002\/anie.201308927<\/a>)<\/p>\n

2012<\/strong><\/p>\n

14. \u00a0 Zhou, D. H.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02012<\/strong>\u00a054(3), 291-305. (http:\/\/doi.org\/10.1007\/s10858-012-9672-z<\/a>)<\/p>\n

2011<\/strong><\/p>\n

13. \u00a0 Wylie, B. J., Sperling, L. J.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02011<\/strong>\u00a0108(41), 16974-9. (http:\/\/doi.org\/10.1073\/pnas.1103728108<\/a>)<\/p>\n

12. \u00a0 Tang, M., Sperling, L. J., Berthold, D. A., Schwieters, C. D., Nesbitt, A. E.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02011<\/strong>\u00a051(3), 227-33. (http:\/\/doi.org\/10.1007\/s10858-011-9565-6<\/a>)<\/p>\n

11. \u00a0 Comellas, G., Lopez, J. J.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02011<\/strong>\u00a0209(2), 131-5. (http:\/\/doi.org\/10.1016\/j.jmr.2010.12.011<\/a>)<\/p>\n

10. \u00a0 Comellas, G., Lemkau, L. R.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02011<\/strong>\u00a0411(4), 881-95. (http:\/\/doi.org\/10.1016\/j.jmb.2011.06.026<\/a>)<\/p>\n

9. \u00a0 Boettcher, J. M., Davis-Harrison, R. L., Clay, M. C.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02011<\/strong>\u00a050(12), 2264-73. (http:\/\/doi.org\/10.1021\/bi1013694<\/a>)<\/p>\n

2010<\/strong><\/p>\n

8. \u00a0 Sperling, L. J.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02010<\/strong>\u00a046(2), 149-55. (http:\/\/doi.org\/10.1007\/s10858-009-9389-9<\/a>)<\/p>\n

7.\u00a0\u00a0 Nieuwkoop, A. J.<\/strong>\u00a0and Rienstra, C. M. “Supramolecular protein structure determination by site-specific long-range intermolecular solid state NMR spectroscopy” J. Am. Chem. Soc.\u00a02010<\/strong>\u00a0132(22), 7570-1. (http:\/\/doi.org\/10.1021\/ja100992y<\/a>)<\/p>\n

6. \u00a0 Nielsen, A. B., Straaso, L. A.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02010<\/strong>\u00a01(13), 1952-6. (http:\/\/doi.org\/10.1021\/jz100564j<\/a>)<\/p>\n

5. \u00a0 Kijac, A., Shih, A. Y.,\u00a0Nieuwkoop, A. J.<\/strong>, Schulten, K., Sligar, S. G. and Rienstra, C. M. “Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance” Biochemistry.\u00a02010<\/strong>\u00a049(43), 9190-8. (http:\/\/doi.org\/10.1021\/bi1013722<\/a>)<\/p>\n

2009<\/strong><\/p>\n

4.\u00a0\u00a0 Nieuwkoop, A. J.<\/strong>, 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.\u00a02009<\/strong>\u00a0131(9), 095101. (http:\/\/doi.org\/10.1063\/1.3211103<\/a>)<\/p>\n

2008<\/strong><\/p>\n

3. \u00a0 Franks, W. T., Wylie, B. J., Schmidt, H. L.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02008<\/strong>\u00a0105(12), 4621-6. (http:\/\/doi.org\/10.1073\/pnas.0712393105<\/a>)<\/p>\n

2007<\/strong><\/p>\n

2. \u00a0 Zhou, D. H., Shea, J. J.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02007<\/strong>\u00a046(44), 8380-3. (http:\/\/doi.org\/10.1002\/anie.200702905<\/a>)<\/p>\n

 <\/p>\n

1. \u00a0 Graesser, D. T., Wylie, B. J.,\u00a0Nieuwkoop, A. J.<\/strong>, 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.\u00a02007<\/strong>\u00a045 Suppl 1(S129-34. (http:\/\/doi.org\/10.1002\/mrc.2126<\/a>)<\/p>\n","protected":false},"excerpt":{"rendered":"

2025 37. Ogbodo, R.; Ansar, I.; Adu, C.; Lall-Ramnarine, S.I.; Wishart, J.F.; Nieuwkoop, A.J.; Margulis, C.J.; Tethered from the head and from the tail; the structure of hydroxyl-functionalized ionic liquids … Read More<\/a><\/p>\n","protected":false},"author":1290,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"class_list":["post-591","page","type-page","status-publish","hentry"],"acf":[],"yoast_head":"\nPublications - Nieuwkoop Lab<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/sites.rutgers.edu\/nieuwkoop-lab\/publications\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Publications - Nieuwkoop Lab\" \/>\n<meta property=\"og:description\" content=\"2025 37. 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