Department of Molecular Biophysics (Adam Lange)

Reviews

[86] J.-P. Demers, P. Fricke, C. Shi, V. Chevelkov, and A. Lange, Structure determination of supra-molecular assemblies by solid-state NMR: practical considerations, Progress in NMR Spectroscopy, in press.

[85] P. Fricke, V. Chevelkov, C. Shi, and A. Lange, Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes, Journal of Magnetic Resonance, 253 (2015), pp. 2-9.

[84] A. Loquet, B. Habenstein, and A. Lange, Structural investigations of molecular machines by solid-state NMR, Accounts of Chemical Research, 46 (2013), pp. 2070-2079.

[83] A. Loquet, B. Habenstein, J.-P. Demers, S. Becker, and A. Lange, Structure d’une nanomachine bactérienne, médecine/sciences, 28 (2012), pp. 926-928.

[82] J.-P. Demers, V. Chevelkov, and A. Lange, Progress in correlation spectroscopy at ultra-fast magic-angle spinning: Basic building blocks and complex experiments for the study of protein structure and dynamics, Solid State Nuclear Magnetic Resonance, 40 (2011), pp. 101-113.

[81] A. Lange and B. H. Meier, Fungal prion proteins studied by solid-state NMR, Comptes Rendus Chimie, 11 (2008), pp. 332-339.

[80] A. Lange and M. Baldus, Membrane proteins studied by solid-state NMR, Structural biology of membrane proteins, Royal Society of Chemistry, Cambridge (2006), pp. 118-130.

[79] A. Lange and M. Baldus, Novel solid-state NMR methods for structural studies on G protein-coupled receptors, G protein-coupled receptors in drug discovery, Taylor and Francis, Boca Raton (2006), pp. 297-314.

[78] S. Luca, H. Heise, A. Lange, and M. Baldus, Investigation of ligand-receptor systems by high-resolution solid-state NMR: Recent progress and perspectives, Archiv der Pharmazie, 338 (2005), pp. 217-228.

Articles

2018

[77] M. Zinke, P. Fricke, S. Lange, S. Zinn-Justin, and A. Lange, Protein-protein interfaces probed by methyl-labeling and proton-detected solid-state NMR spectroscopy, ChemPhysChem, in press.

[76] S. Hwang, P. Fricke, M. Zinke, K. Giller, J. S. Wall, D. Riedel, S. Becker, and A. Lange, Comparison of the 3D structures of mouse and human α-synuclein fibrils by solid-state NMR and STEM, Journal of Structural Biology, in press.

[75] C. Shi, Y. He, K. Hendriks, B. L. de Groot, X. Cai, C. Tian, A. Lange*, and H. Sun*, A single NaK channel conformation is not enough for non-selective ion conduction, Nature Communications, 9 (2018), 717.

2017

[74] V. Chevelkov, K. Giller, S. Becker, and A. Lange, Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR, Journal of Magnetic Resonance, 283 (2017), pp. 110-116.

[73] M. Zinke, P. Fricke, C. Samson, S. Hwang, J. S. Wall, S. Lange, S. Zinn-Justin, and A. Lange, Bacteriophage tail tube assembly studied by proton-detected 4D solid-state NMR, Angewandte Chemie-International Edition, 56 (2017), pp. 9497-9501.

[72] M. Salvi, B. Schomburg, K. Giller, S. Graf, G. Unden, S. Becker, A. Lange*, and C. Griesinger*, Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor, Proceedings of the National Academy of Sciences, 114 (2017), pp. 3115-3120.

[71] S. Xiang, N. Kulminskaya, B. Habenstein, J. Biernat, K. Tepper, M. Paulat, C. Griesinger, S. Becker, A. Lange, E. Mandelkow, and R. Linser, A two-component adhesive: tau fibrils arise from a combination of a well-defined motif and conformationally flexible interactions, Journal of the American Chemical Society, 139 (2017), pp. 2639-2646.

[70] P. Fricke, V. Chevelkov, M. Zinke, K. Giller, S. Becker, and A. Lange, Backbone assignment of perdeuterated proteins by solid-state NMR using proton-detection and ultrafast magic-angle spinning, Nature Protocols, 12 (2017), pp. 764-782.

[69] C. Samson, F. Celli, K. Hendriks, M. Zinke, N. Essawy, I. Herrada, A. A. Arteni, F. X. Theillet, B. Alpha-Bazin, J. Armengaud, C. Coirault, A. Lange, and S. Zinn-Justin, Emerin self-assembly mechanism: role of the LEM domain, FEBS Journal, 284 (2017), pp. 338-352.

2016

[68] R. Briones, C. Weichbrodt, L. Paltrinieri, I. Mey, S. Villinger, K. Giller, A. Lange, M. Zweckstetter, C. Griesinger, S. Becker, C. Steinem, and B. L. de Groot, Voltage dependence of conformational dynamics and subconducting states of VDAC-1, Biophysical Journal, 111 (2016), pp. 1223-1234.

[67] P. Fricke, D. Mance, V. Chevelkov, K. Giller, S. Becker, M. Baldus, and A. Lange, High resolution observed in 800 MHz DNP spectra of extremely rigid type III secretion needles, Journal of Biomolecular NMR, 65 (2016), pp. 121-126.

[66] A.-C. Pöppler, J.-P. Demers, M. Malon, A. P. Singh, H. W. Roesky, Y. Nishiyama, and A. Lange, Ultra-fast magic angle spinning: benefits for the acquisition of ultra-wideline NMR spectra of heavy spin-1/2 nuclei, ChemPhysChem, 17 (2016), pp. 812-816.

2015

[65] C. Shi, P. Fricke, L. Lin, V. Chevelkov, M. Wegstroth, K. Giller, S. Becker, M. Thanbichler, and A. Lange, Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR, Science Advances, 1 (2015), e1501087.

[64] B. Habenstein, A. Loquet, S. Hwang, K. Giller, S. K. Vasa, S. Becker, M. Habeck, and A. Lange, Hybrid structure of the type 1 pilus of uropathogenic Escherichia coli, Angewandte Chemie-International Edition, 54 (2015), pp. 11691-11695.

[63] H. K. Fasshuber, N. A. Lakomek, B. Habenstein, A. Loquet, C. Shi, K. Giller, S. Wolff, S. Becker, and A. Lange, Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR, Protein Science, 24 (2015), pp. 592-598.

[62] V. Chevelkov, S. Xiang, K. Giller, S. Becker, A. Lange, and B. Reif, Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization, Journal of Biomolecular NMR, 61 (2015), pp. 151-160.

[61] H. K. Fasshuber, J.-P. Demers, V. Chevelkov, K. Giller, S. Becker, and A. Lange, Specific 13C labeling of leucine, valine and isoleucine methyl groups for unambiguous detection of long-range restraints in protein solid-state NMR studies, Journal of Magnetic Resonance, 252 (2015), pp. 10-19.

[60] J.-P. Demers, V. Vijayan, and A. Lange, Recovery of bulk proton magnetization and sensitivity enhancement in ultrafast magic-angle spinning solid-state NMR, Journal of Physical Chemistry B, 119 (2015), pp. 2908-2920.

[59] S. Vasa, L. Lin, C. Shi, B. Habenstein, D. Riedel, J. Kühn, M. Thanbichler, and A. Lange, β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR, Proceedings of the National Academy of Sciences, 112 (2015), E127-E136.

[58] Z. Gattin, R. Schneider, Y. Laukat, K. Giller, E. Maier, M. Zweckstetter, C. Griesinger, R. Benz, S. Becker, and A. Lange, Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2, Journal of Biomolecular NMR, 61 (2015), pp. 311-320.

2014

[57] X. Yao, U. H. Dürr, Z. Gattin, Y. Laukat, R. L. Narayanan, A. K. Brückner, C. Meisinger, A. Lange, S. Becker, and M. Zweckstetter, NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins, PLoS One, 9 (2014), e112374.

[56] S. Xiang, V. Chevelkov, S. Becker, and A. Lange, Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data, Journal of Biomolecular NMR, 60 (2014), pp. 85-90.

[55] J.-P. Demers, B. Habenstein, A. Loquet, S. K. Vasa, K. Giller, S. Becker, D. Baker, A. Lange* and N. G. Sgourakis*, High-resolution structure of the Shigella type-III secretion needle determined by solid-state NMR and cryo-electron microscopy, Nature Communications, 5 (2014), 4976.

[54] K. F. Kalz, N. Kindermann, S. Xiang, A. Kronz, A. Lange, and F. Meyer, Revisiting the Synthesis and Elucidating the Structure of Potassium Cyclopentadienyldicarbonylruthenate, K[CpRu(CO)2], Organometallics, 33 (2014), pp. 1475-1479.

[53] S. Villinger, K. Giller, M. Bayrhuber, A. Lange, C. Griesinger, S. Becker, and M. Zweckstetter, Nucleotide interactions of the human voltage-dependent anion channel, Journal of Biological Chemistry, 289 (2014), pp. 13397-13406.

[52] V. Chevelkov, B. Habenstein, A. Loquet, K. Giller, S. Becker, and A. Lange, Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins, Journal of Magnetic Resonance, 242 (2014), pp. 180-188.

[51] C. Shi, H. K. Fasshuber, V. Chevelkov, S. Xiang, B. Habenstein, S. K. Vasa, S. Becker, and A. Lange, BSH-CP based 3D solid-state NMR experiments for protein resonance assignment, Journal of Biomolecular NMR, 59 (2014), pp. 15-22.

[50] D. Matthes, V. Daebel, K. Meyenberg, D. Riedel, G. Heim, U. Diederichsen, A. Lange, and B. L. de Groot, Spontaneous aggregation of the insulin-derived steric zipper peptide VEALYL results in different aggregation forms with common features, Journal of Molecular Biology, 426 (2014), pp. 362-376.

[49] P. P. Samuel, Y. Li, H. W. Roesky, V. Chevelkov, A. Lange, A. Burkhardt, and B. Dittrich, Synthetic access to a hydrocarbon-soluble trifluorinated Ge(II) compound and its Sn(II) congener, Journal of the American Chemical Society, 136 (2014), pp. 1292-1295.

[48] P. Fricke, J.-P. Demers, S. Becker, and A. Lange, Studies on the MxiH protein in T3SS needles using DNP-enhanced ssNMR spectroscopy, ChemPhysChem, 15 (2014), pp. 57-60.

2013

[47] A. Loquet, B. Habenstein, V. Chevelkov, S. K. Vasa, K. Giller, S. Becker, and A. Lange, Atomic structure and handedness of the building block of a biological assembly, Journal of the American Chemical Society, 135 (2013), pp. 19135-19138.

[46] V. Chevelkov, C. Shi, H. K. Fasshuber, S. Becker, and A. Lange,  Efficient band-selective homonuclear CO-CA cross-polarization in protonated proteins, Journal of Biomolecular NMR, 56 (2013), pp. 303-311.

[45] J.-M. Lopez del Amo, D. Schneider, A. Loquet, A. Lange, and B. Reif, Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: perspectives for DNP, Journal of Biomolecular NMR, 56 (2013), pp. 359-363.

[44] J.-P. Demers, N. G. Sgourakis, R. Gupta, A. Loquet, K. Giller, D. Riedel, B. Laube, M. Kolbe, D. Baker, S. Becker, and A. Lange, The common structural architecture of Shigella flexneri and Salmonella typhimurium type three secretion needles, PLOS Pathogens, 9 (2013), e1003245.

[43] V. Chevelkov, K. Giller, S. Becker, and A. Lange,  Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization, Journal of Magnetic Resonance, 230 (2013), pp. 205-211.

[42] G. Lv, H. K. Faßhuber, A. Loquet, J.-P. Demers, V. Vijayan, K. Giller, S. Becker, and A. Lange, A straightforward method for stereospecific assignment of val and leu prochiral methyl groups by solid-state NMR: Scrambling in the [2-13C]glucose labeling scheme, Journal of Magnetic Resonance, 228 (2013), pp. 45-49.

[41] B. Habenstein, A. Loquet, K. Giller, S. Becker, and A. Lange, Structural characterization of supramolecular assemblies by 13C spin dilution and 3D solid-state NMR, Journal of Biomolecular NMR, 55 (2013), pp. 1-9.

2012

[40] A. P. Singh, R. S. Ghadwal, H. W. Roesky, J. J. Holstein, B. Dittrich, J.-P. Demers, V. Chevelkov, and A. Lange, Lewis base mediated dismutation of trichlorosilane, Chemical Communications, 48 (2012), pp. 7574-7576.

[39] U. Zachariae, R. Schneider, R. Briones, Z. Gattin, J.-P. Demers, K. Giller, E. Maier, M. Zweckstetter, C. Griesinger, S. Becker, R. Benz, B. L. de Groot, and A. Lange, β-barrel mobility underlies closure of the voltage-dependent anion channel, Structure, 20 (2012), pp. 1540-1549.

[38] V. Daebel, S. Chinnathambi, J. Biernat, M. Schwalbe, B. Habenstein, A. Loquet, E. Akoury, K. Tepper, H. Müller, M. Baldus, C. Griesinger, M. Zweckstetter, E. Mandelkow, V. Vijayan, and A. Lange, β-sheet core of tau paired helical filaments revealed by solid-state NMR, Journal of the American Chemical Society, 134 (2012), pp. 13982-13989.

[37] G. Lv, A. Kumar, K. Giller, M. L. Orcellet, D. Riedel, C. O. Fernández, S. Becker, and A. Lange, Structural comparison of mouse and human α-synuclein amyloid fibrils by solid-state NMR, Journal of Molecular Biology, 420 (2012), pp. 99-111.

[36] A. Loquet, N. G. Sgourakis, R. Gupta, K. Giller, D. Riedel, C. Goosmann, C. Griesinger, M. Kolbe, D. Baker, S. Becker, and A. Lange, Atomic model of the type III secretion system needle, Nature, 486 (2012), pp. 276-279.

[35] S. Khan, P. P. Samuel, R. Michel, J. M. Dieterich, R. A. Mata, J.-P. Demers, A. Lange, H. W. Roesky, and D. Stalke, Monomeric Sn(II) and Ge(II) hydrides supported by a tridentate pincer-based ligand, Chemical Communications, 48 (2012), pp. 4890-4892.

[34] A. P. Singh, H. W. Roesky, E. Carl, D. Stalke, J.-P. Demers, and A. Lange, Lewis base mediated autoionization of GeCl2 and SnCl2, Journal of the American Chemical Society, 134 (2012), pp. 4998-5003.

[33] A.-C. Pöppler, M. M. Meinholz, H. Faßhuber, A. Lange, M. John, and D. Stalke, Mixed crystalline lithium organics and interconversion in solution, Organometallics, 31 (2012), pp. 42-45.

2011

[32] S. Khan, R. Michel, J. M. Dieterich, R. A. Mata, H. W. Roesky, J.-P. Demers, A. Lange, and D. Stalke, Preparation of RSn(I)–Sn(I)R with two unsymmetrically coordinated Sn(I) atoms and subsequent gentle activation of P4, Journal of the American Chemical Society, 133 (2011), pp. 17889-17894.

[31] T. Tatic, S. Hermann, M. John, A. Loquet, A. Lange, and D. Stalke, Pure α-metallated benzyllithium from a single-crystal-to-single-crystal transition, Angewandte Chemie-International Edition, 50 (2011), pp. 6666-6669.

[30] A. Loquet, G. Lv, K. Giller, S. Becker, and A. Lange, 13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies, Journal of the American Chemical Society, 133 (2011), pp. 4722-4725.

[29] S. S. Sen, S. Khan, H. W. Roesky, D. Kratzert, K. Meindl, J. Henn, D. Stalke, J.-P. Demers, and A. Lange, Zwitterionic Si-C-Si-P and Si-P-Si-P four-membered rings with two-coordinate phosphorus atoms, Angewandte Chemie-International Edition, 50 (2011), pp. 2322-2325.

2010

[28] H. Van Melckebeke, P. Schanda, J. Gath, C. Wasmer, R. Verel, A. Lange, B. H. Meier, and A. Böckmann, Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR, Journal of Molecular Biology, 405 (2010), pp. 765-772.

[27] S. Villinger, R. Briones, K. Giller, U. Zachariae, A. Lange, B. L. de Groot, C. Griesinger, S. Becker, and M. Zweckstetter, Functional dynamics in the voltage-dependent anion channel, Proceedings of the National Academy of Sciences, 107 (2010), pp. 22546-22551.

[26] A. Loquet, K. Giller, S. Becker, and A. Lange, Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy, Journal of the American Chemical Society, 132 (2010), pp. 15164-15166.

[25] H. Van Melckebeke, C. Wasmer, A. Lange, E. Ab, A. Loquet, A. Böckmann, and B. H. Meier, Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy, Journal of the American Chemical Society, 132 (2010), pp. 13765-13775.

[24] J.-P. Demers, V. Vijayan, S. Becker, and A. Lange, Tailored low-power cross-polarization under fast magic-angle spinning, Journal of Magnetic Resonance, 205 (2010), pp. 216-223.

[23] O. Poyraz, H. Schmidt, K. Seidel, F. Delissen, C. Ader, H. Tenenboim, C. Goosmann, B. Laube, A. F. Thünemann, A. Zychlinsky, M. Baldus, A. Lange*, C. Griesinger, and M. Kolbe*, Protein refolding is required for assembly of the type three secretion needle, Nature Structural & Molecular Biology, 17 (2010), pp. 788-792.

[22] A. Sachse, S. Demeshko, S. Dechert, V. Daebel, A. Lange, and F. Meyer, Highly preorganized pyrazolate-bridged palladium(II) and nickel(II) complexes in bimetallic norbornene polymerization, Dalton Transactions, 39 (2010), pp. 3903-3914.

[21] R. Schneider, M. Etzkorn, K. Giller, V. Daebel, J. Eisfeld, M. Zweckstetter, C. Griesinger, S. Becker, and A. Lange, The native conformation of the human VDAC1 N terminus, Angewandte Chemie-International Edition, 49 (2010), pp. 1882-1885.

[20] R. Schneider, K. Seidel, M. Etzkorn, A. Lange, S. Becker, and M. Baldus, Probing molecular motion by double-quantum (13C, 13C) solid-state NMR spectroscopy: Application to ubiquitin, Journal of the American Chemical Society, 132 (2010), pp. 223-233.

2009

[19] H. Y. Kim, M. K. Cho, A. Kumar, E. Maier, C. Siebenhaar, S. Becker, C. O. Fernandez, H. A. Lashuel, R. Benz, A. Lange, and M. Zweckstetter, Structural properties of pore-forming oligomers of α-synuclein, Journal of the American Chemical Society, 131 (2009), pp. 17482-17489.

[18] V. Vijayan, J.-P. Demers, J. Biernat, E. Mandelkow, S. Becker, and A. Lange, Low-power solid-state NMR experiments for resonance assignment under fast magic-angle spinning, ChemPhysChem, 10 (2009), pp. 2205-2208.

[17] A. Lange, Z. Gattin, H. Van Melckebeke, C. Wasmer, A. Soragni, W. F. van Gunsteren, and B. H. Meier, A combined solid-state NMR and MD characterization of the stability and dynamics of the HET-s(218-289) prion in its amyloid conformation, ChemBioChem, 10 (2009), pp. 1657-1665.

[16] A. Lange, I. Scholz, T. Manolikas, M. Ernst, and B. H. Meier, Low-power cross polarization in fast magic-angle spinning NMR experiments, Chemical Physics Letters, 468 (2009), pp. 100-105.

2008

[15] C. Wasmer, A. Soragni, R. Sabaté, A. Lange, R. Riek, and B. H. Meier, Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra, Angewandte Chemie-International Edition, 47 (2008), pp. 5839-5841.

[14] J. Korukottu, R. Schneider, V. Vijayan, A. Lange, O. Pongs, S. Becker, M. Baldus, and M. Zweckstetter, High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy, PLoS ONE, 3 (2008), e2359.

[13] C. Ader, R. Schneider, S. Hornig, P. Velisetty, E. M. Wilson, A. Lange, K. Giller, I. Ohmert, M. F. Martin-Eauclaire, D. Trauner, S. Becker, O. Pongs, and M. Baldus, A structural link between inactivation and block of a K+ channel, Nature Structural & Molecular Biology, 15 (2008), pp. 605-612.

[12] R. Schneider, C. Ader, A. Lange, K. Giller, S. Hornig, O. Pongs, S. Becker, and M. Baldus, Solid-state NMR spectroscopy applied to a chimeric potassium channel in lipid bilayers, Journal of the American Chemical Society, 130 (2008), pp. 7427-7435.

[11] U. Zachariae, R. Schneider, P. Velisetty, A. Lange, D. Seeliger, S. J. Wacker, Y. Karimi-Nejad, G. Vriend, S. Becker, O. Pongs, M. Baldus, and B. L. de Groot, The molecular mechanism of toxin-induced conformational changes in a potassium channel: Relation to C-type inactivation, Structure, 16 (2008), pp. 747-754.

[10] C. Wasmer*, A. Lange*, H. Van Melckebeke*, A. B. Siemer, R. Riek, and B. H. Meier, Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core, Science, 319 (2008), pp. 1523-1526.

2007

[9] A. Lange, T. Schupp, F. Petersen, T. Carlomagno, and M. Baldus, High-resolution solid-state NMR structure of an anticancer agent, ChemMedChem, 2 (2007), pp. 522-527.

2006

[8] A. Lange, K. Giller, O. Pongs, S. Becker, and M. Baldus, Two-dimensional solid-state NMR applied to a chimeric potassium channel, Journal of Receptors and Signal Transduction, 26 (2006), pp. 379-393.

[7] A. Lange, K. Giller, S. Hornig, M. F. Martin-Eauclaire, O. Pongs, S. Becker, and M. Baldus, Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR, Nature, 440 (2006), pp. 959-962.

2005

[6] A. Lange, S. Becker, K. Seidel, K. Giller, O. Pongs, and M. Baldus, A concept for rapid protein-structure determination by solid-state NMR spectroscopy, Angewandte Chemie-International Edition, 44 (2005), pp. 2089-2092.

2004

[5] K. Seidel, A. Lange, S. Becker, C. E. Hughes, H. Heise, and M. Baldus, Protein solid-state NMR resonance assignments from 13C-13C correlation spectroscopy, Physical Chemistry Chemical Physics, 6 (2004), pp. 5090-5093.

[4] M. Etzkorn, A. Böckmann, A. Lange, and M. Baldus, Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling, Journal of the American Chemical Society, 126 (2004), pp. 14746-14751.

2003

[3] A. Böckmann, A. Lange, A. Galinier, S. Luca, N. Giraud, M. Juy, H. Heise, R. Montserret, F. Penin, and M. Baldus, Solid-state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh, Journal of Biomolecular NMR, 27 (2003), pp. 323-339.

[2] A. Lange, K. Seidel, L. Verdier, S. Luca, and M. Baldus, Analysis of proton-proton transfer dynamics in rotating solids and their use for 3D structure determination, Journal of the American Chemical Society, 125 (2003), pp. 12640-12648.

2002

[1] A. Lange, S. Luca, and M. Baldus, Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids, Journal of the American Chemical Society, 124 (2002), pp. 9704-9705.

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