1. R. Linser, V. Chevelkov, A. Diehl, B. Reif, “Sensitivity Enhancement Using Paramagnetic Relaxation in MAS Solid-State NMR of Perdeuterated Proteins”, J. Magn. Reson. 189, 209–216 (2007).
  2. R. Linser, U. Fink, B. Reif, “Proton-Detected Scalar Coupling Based Assignment Strategies in MAS Solid-State NMR Spectroscopy Applied to Perdeuterated Proteins”, J. Magn. Reson. 193, 89–93 (2008).
  3. A. Krushelnitsky, E. de Azevedo, R. Linser, B. Reif, K. Saalwaechter, D. Reichert, “Direct Observation of Millisecond to Second Motions in Proteins by Dipolar CODEX NMR”, J. Am. Chem. Soc. 131, 12097–12099 (2009).
  4. R. Linser, U. Fink, B. Reif, “Probing Surface Accessibility of Proteins Using Paramagnetic Relaxation in MAS solid-state NMR Spectroscopy”, J. Am. Chem. Soc. 131 (38), 13703–13708 (2009).
  5. Ü. Akbey, S. Lange, W. T. Franks, R. Linser, K. Rehbein, A. Diehl, B. J. van Rossum, B. Reif, H. Oschkinat, „Optimum Levels of Exchangeable Protons in Perdeuterated Proteins for Proton Detection in MAS Solid-State NMR Spectroscopy“, J. Biomol. NMR 46, 67–73 (2009).
  6. R. Linser, U. Fink, B. Reif, “Narrow Carbonyl Linewidths of Proton-Diluted Proteins Facilitate NMR Assignments in the Solid State”, J. Biomol. NMR 47 (1), 1–6 (2010).
  7. V. Agarwal, R. Linser, U. Fink, K. Fälber, B. Reif, „Identification of Hydroxyl Protons and Characterization of Exchange Behaviour and Hydrogen Bonding in a Microcrystalline Protein”, J. Am. Chem. Soc. 132 (9), 3187–3195 (2010).
  8. V. Chevelkov, Y. Xue, R. Linser, N. Skrynnikov, B. Reif, „Comparison of Solid-State Dipolar Couplings and Solution Relaxation Data Provides Insight into Protein Backbone Dynamics”, J. Am. Chem. Soc. 132 (14), 5015–5017 (2010).
  9. R. Linser, U. Fink, B. Reif, “Detection of dynamic regions in biological solids enabled by spin-state selective NMR experiments”, J. Am. Chem. Soc. 132 (26), 8891–8893 (2010).
  10. R. Linser, “MAS Solid-State NMR on Biomolecules: Development and Application of New Methodology”, Südwestdeutscher Verlag für Hochschulschriften AG Co. KG, Saarbrücken, ISBN-13: 9783838125480.
  11. R. Linser*, B. Bardiaux, V. Higman, U. Fink, B. Reif*, “Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H−1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy”, J. Am. Chem. Soc. 133 (15), 5905–5912 (2011).
  12. R. Linser, M. Dasari, U. Fink, P. Schmieder, J.-M. Lopez del Amo, S. Marcovic, M. Hiller, H. Oschkinat, D. Oesterheld, B. Reif, “Proton detected solid state NMR of fibrillar and membrane proteins”, Angew. Chem., Int. Ed. 50 (19), 4508–4512 (2011);
    Cover, Angew. Chem. Int. Ed. 50 (19), 4237 (2011).

    R. Linser, M. Dasari, U. Fink, P. Schmieder, J.-M. Lopez del Amo, S. Marcovic, M. Hiller, H. Oschkinat, D. Oesterheld, B. Reif, “Festkörper-NMR-Spektroskopie mit Protonendetektion an fibrillären Proteinen und Membranproteinen”, Angew. Chem. 123 (19), 4601–4605 (2011);
    Cover, Angew. Chem. 123 (19), 4325 (2011).
  13. R. Linser, “Sidechain to backbone correlation in perdeuterated proteins through combined excitation and long-range magnetization transfer.”, J. Biomol. NMR 51 (3), 221–226 (2011).
  14. R. L. Holmes, J. A. Campbell, R. Linser, J. M. Hook, R. P. Burford, “In-situ preparation of poly(2-hydroxyethyl methacrylate)-titania hybrids using γ-radiation”, Polymer 52 (20), 4471–4479 (2011).
  15. R. Linser, “Backbone Assignment of Perdeuterated Proteins Using Long-Range H/C-Dipolar Transfers”, J. Biomol. NMR 52 (2), 151–158 (2012).
  16. V. Morris, R. Linser†, K. L. Wilde, A. P. Duff, M. Sunde, A. Kwan, “Solid-state NMR spectroscopy of functional amyloid from a fungal hydrophobin: A well-ordered β-sheet core amidst structural heterogeneity”, Angew. Chem. Int. Ed. 51 (50), 12621–12625 (2012).
    († Shared first-authorship.)

    V. Morris, R. Linser †, K. L. Wilde, A. P. Duff, M. Sunde, A. Kwan, “Festkörper-NMR-Spektroskopie an funktionellen Amyloiden eines Pilz-Hydrophobins: Hinweise auf einen geordneten β-Faltblattkern bei genereller struktureller Heterogenität“, Angew. Chem. 124 (50), 12791–12795 (2012). († Shared first-authorship.)
  17. V. Agarwal, R. Linser, M. Dasari, U. Fink, J.-M. Lopez Del Amo, B. Reif, “Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure.” Phys. Chem. Chem. Phys. 15, 12551–12557 (2013).
  18. A. Mainz, T. Religa, R. Sprangers, R. Linser, L. E. Kay, B. Reif, “NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond”, Angew. Chem. Int. Ed. 52 (33), 8746–8751 (2013).

    A. Mainz, T. Religa, R. Sprangers, R. Linser, L. E. Kay, B. Reif, “NMR-Spektroskopie an löslichen Proteinkomplexen mit Molekulargewicht im Mega-Dalton-Bereich”, Angew. Chem. 125 (33), 8909–8914 (2013).
  19. S. M. F. Rabbi, R. Linser, J. M. Hook, B. R. Wilson, P. V. Lockwood, H. Daniel, I. M. Young, “Characterization of soil organic matter in aggregates and size-density fractions by solid state 13C CPMAS NMR spectroscopy”, Commun. Soil Sci. Plan. 45 (11) 1523–1537 (2014).
  20. R. Linser, R. Sarkar, A. Krushelnitzky, A. Mainz, B. Reif, “Dynamics in the Solid State: Perspectives for the Investigation of Amyloid Aggregates, Membrane Proteins, and Soluble Protein Complexes”, J. Biomol. NMR 59 (1), 1–14 (2014).
  21. R. Linser*, V. Gelev, F. Hagn, S. G. Hyberts, H. Arthanari, G. Wagner*, “Selective methyl labeling of eukaryotic membrane proteins using cell-free expression”, J. Am. Chem. Soc. 136 (32), 11308–11310 (2014),
    Cover: J. Am. Chem. Soc., 2014, 136 (32), front page.
    Spotlights article: J. Am. Chem. Soc., 2014, 136 (32), 11197.
  22. C. H. Chia, S. D. Joseph, A. Rawal, R. Linser, J. M. Hook, P. Munroe, “Microstructural Characterization of White Charcoal”, J. Anal. Appl. Pyrol. 109, 215-221 (2014).
  23. A. Trebugov†, R. Linser†, K. Q. Vuong, A. Rawal, J. Gehman, B. Messerle, “Solid-State NMR Structure Characterization of a 13CO-Labeled Ir(I) Complex with a P,N‑Donor Ligand Including Ultrafast MAS Methods”, Inorg. Chem. 53, 7146−7153 (2014).
    († Shared first-authorship)
  24. R. Linser*, B. Bardiaux, S. G. Hyberts, A. Kwan, V. Morris, M. Sunde, G. Wagner, “Solid-State NMR Structure Determination from Diagonal-Compensated, Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints”, J. Am. Chem. Soc. 136 (31), 11002–11010 (2014).
  25. S. Roy, K. C. Mondal, L. Krause, P. Stollberg, R. Herbst-Irmer, D. Stalke, J. Meyer, A. C. Stückl, B. Maity, D. Koley, S. K. Vasa, S. Q. Xiang, R. Linser, H. W. Roesky, “Electron-Induced Conversion of Silylones to Six-membered Cyclic Silylenes”, J. Am. Chem. Soc., 136 (48), 16776–16779 (2014).
  26. S. Xiang, K. Grohe, P. Rovó, S. K. Vasa, K. Giller, S. Becker, R. Linser, “Sequential backbone assignment based on direct amide-to-amide correlation experiments”, J. Biomol. NMR, 62 (3), 303–311 (2015).
  27. S. Roy, B. Dittrich, T. Mondal, D. Koley, A. C. Stückl, B. Schwederski, W. Kaim, M. John, S. K. Vasa, R. Linser, H. Roesky, “Carbene Supported Dimer of Heavier Ketenimine Analogue with P and Si Atoms”, J. Am. Chem. Soc., 137 (19), 6180–6183 (2015).
  28. K. C. Mondal, S. Roy, B. Dittrich, D. Koley, B. Maity, S. Dutta, R. Linser, S. K. Vasa, S. Dechert, H. Roesky, “A Soluble Molecular Variant of the Semiconducting Silicondiselenide”, Chem. Sci., 6, 5230–5234 (2015).
  29. N. Kulminskaya, S. K. Vasa, K. Giller, S. Becker, R. Linser, “Asynchronous through-bond homonuclear isotropic mixing: Application to carbon-carbon transfer in perdeuterated proteins under MAS”, J. Biomol. NMR, 63 (3), 245-253 (2015).
  30. R. Linser*, N. Salvi, R. Briones, P. Rovó, B. de Groot, G. Wagner*,The Membrane Anchor of the Transcriptional Activator SREBP is Characterized by Intrinsic Conformational Flexibility”, Proc. Natl. Acad. Sci. U.S.A, 112 (40) 12390-12395 (2015).
  31. P. Rovó, K. Grohe, K. Giller, S. Becker, R. Linser, “Proton Transverse Relaxation as a Sensitive Probe for Structure Determination in Solid Proteins”, ChemPhysChem,, 16 (18), 3791–3796 (2015).
    Cover: ChemPhysChem, 16 (18), 3739 (2015).
    ”Cover Profile” article: ChemPhysChem, 16 (18), 3743 (2015).
  32. N. Kulminskaya, S. K. Vasa, K. Giller, S. Becker, A. Kwan, M. Sunde, R. Linser, “Access to side-chain carbon information in deuterated solids under ultra-fast MAS through non-rotor-synchronized mixing”, ChemComm, 52 (2), 268-271 (2016).
    Back cover feature: ChemComm, 52 (2), 419 (2016).
  33. S. K. Vasa, P. Rovó, K. Giller, S. Becker, R. Linser,Access to Aliphatic Protons as Reporters in Non-Deuterated Proteins by Second-Order Transfer”, PhysChemChemPhys, 18, 8359 – 8363 (2016).
    Back cover: PhysChemChemPhys 18, 8754 (2016).
  34. J. I. Schweizer, M. G. Scheibel, M. Diefenbach, F. Neumeyer, C. Würtele, N. Kulminskaya, R. Linser, N. Auner, S. Schneider, M. C. Holthausen, “A Disilene Base Adduct with a Dative Si–Si Single Bond”, Angew. Chem., Int. Ed., 55 (5), 1782-1786 (2016).
  35. S. Xiang, J. Biernat, E. Mandelkow, S. Becker, R. Linser, “Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration”, Chem. Commun., 52, 4002-4005 (2016).
    Cover: Chem. Commun., 52, 3979-3979 (2016)
  36. I. Gonzalo-Juan, D. U. Tulyaganov, C. Balan, R. Linser, J. M. F. Ferreira, R. Riedel, E. Ionescu, “Tailoring the viscoelastic properties of injectable biocomposites: A spectroscopic assessment of the interactions between organic carriers and bioactive glass particles”, Mater. Design, 97, 45-50 (2016).
  37. R. Linser, “Michael L. Johns, Einar O. Fridjonsson, Sarah Vogt, and Agnes Haber (Eds.): Mobile NMR and MRI. Developments and applications.” , Anal. Bioanal. Chem. Anal. Bioanal. Chem. 408 (15), 3929-3931 (2016).
  38. R. Linser, “Protons as sensitive reporters for molecular details.”, in the research report of the Max Planck Society (2016).
  39. J. Cramer, J. Schiebel, T. Wulsdorf, K. Grohe, E. E. Najbauer, F. R. Ehrmann, N. Radeva, N. Zitzer, U. Linne, R. Linser, A. Heine, G. Klebe, “A False-Positive Screening Hit in Fragment-Based Lead Discovery: Watch out for the Red Herring”, Angew. Chem., Int. Ed., 56 (7), 1908–1913 (2017),

    J. Cramer, J. Schiebel, T. Wulsdorf, K. Grohe, E. E. Najbauer, F. R. Ehrmann, N. Radeva, N. Zitzer, U. Linne, R. Linser, A. Heine, G. Klebe, “Falsch-positiver Treffer im Fragment-basierten Wirkstoffdesign: Lass Dich nicht auf die falsche Fährte locken!”, Angew. Chem., 129 (7), 1934–1940 (2017).
  40. S. Xiang, N. Kulminskaya, B. Habenstein, J. Biernat, K. Tepper, M. Paulat, C. Griesinger, S. Becker, A. Lange, E. Mandelkow, R. Linser, “A two-component adhesive: Tau fibrils arise from a combination of a well-defined motif and conformationally flexible interactions”, J. Am. Chem. Soc., 139, 2639−2646 (2017).
  41. G. Jaipuria, A. Leonov, K. Giller, S. K. Vasa, L. Jaremko, M. Jaremko, R. Linser, S. Becker, M. Zweckstetter, “Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structure”, Nature Comm. 8, 14893 (2017).
  42. K. Grohe, K. Tekwani Movellan, S. K. Vasa, K. Giller, S. Becker, R. Linser, “Non-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins”, J. Biomol. NMR, 68 (1), 7-17 (2017).
  43. D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, “Protein conformational dynamics studied by 15N and 1H R1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals”, Solid State Nucl. Mag., 87, 86-95 (2017).
  44. P. Rovó, R. Linser, “Microsecond timescale proton rotating-frame relaxation under magic angle spinning”, J. Phys Chem. 121 (25), 6117–6130 (2017).
  45. D. Fischer, A. von Mankowski, A. Ranft, S. K. Vasa, R. Linser, J. Mannhart, B. V. Lotsch, “ZIF‑8 films prepared by femtosecond pulsed-laser-deposition”, Chem. Mater., 29 (12), 5148–5155 (2017).
  46. R. Linser, “Solid-state NMR spectroscopic trends for supramolecular assemblies and protein aggregates”, invited “Trends” article in Solid state Nucl. Magn. Res., 87:45-53 (2017).
  47. P. Rovó, R. Linser, “Microsecond timescale solid-state backbone dynamics: a combined NMR approach”, ChemPhysChem, 19, 34–39 (2018).
  48. S. K. Vasa, H. Singh, P. Rovó, R. Linser, “Dynamics and interactions of a 29-kDa human enzyme studied by solid-state NMR”, J. Phys. Chem. Lett., 9, 1307−1311 DOI: 10.1021/acs.jpclett.8b00110 (2018). (Link)
  49. S. K. Vasa, P. Rovó, R. Linser, “Protons as versatile reporters in solid-state NMR spectroscopy”, Acc. Chem. Res., 51 (6), 1386-1395 (2018). (Link)
  50. A. Klein, S. K. Vasa, R. Linser, “Automated projection spectroscopy in solid-state NMR", J. Biomol. NMR 72, 163-170 (2018). (Link)
  51. P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, R. Linser, “Mechanistic insights into microsecond timescale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques”, J. Am. Chem. Soc., 141 (2), 858–869, DOI: 10.1021/jacs.8b09258 (2019). (Link)
  52. S. K. Vasa, H. Singh, K.Grohe, R. Linser, "Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration", Angew. Chem. Int. Ed., 58 (17), 5758-5762, DOI: 10.1002/anie.201811714 (2019). (Link) (Cover article: See the picture here!)

    S. K. Vasa, H. Singh, K.Grohe, R. Linser, "Charakterisierung eines großen Enzym‐Wirkstoff‐Komplexes mittels protonendetektierter Festkörper‐NMR ohne Deuterierung", Angew. Chem., 131 (17), 5814-5819, DOI: 10.1002/ange.201902502 (2019). (Link) (Cover-Artikel: Hier geht's zum Bild!)
  53. K. Grohe, H. Singh, S. K. Vasa, B. Söldner, E. Nimerovsky, B. Vögeli, C. M. Rienstra, R. Linser, “Exact distance measurements for structure and dynamics in solid proteins by fast magic angle spinning NMR”, Chem. Commun. 55, 7899–7902 (2019). (Link) (Cover article: See the picture here!)

  54. H. Singh, S. K. Vasa, H. Jangra,  P. Rovó, C. Päslack, C. K. Das, H. Zipse, L. Schäfer, R. Linser, “Fast-microsecond dynamics of the protein-water network in the active site of human carbonic anhydrase II by solid-state NMR spectroscopy.” J. Am. Chem. Soc., 141 (49), 19276-19288, DOI: 10.1021/jacs.9b05311 (2019). (Link) (Cover article: See the picture here!)

  55. E. Burakova, A. Klein, S. K. Vasa, R. Linser, “Non-uniform sampling in quantitative assessment of heterogeneous solid-state NMR line shapes”, J. Biomol. NMR, 74, 7182, DOI: 10.1007/s10858-019-00291-z (2020). (Link)

  56. K. Grohe, S. Patel, C. Hebrank, S. Medina, A. Klein, P. Rovó, S. K. Vasa, H. Singh, B. Vögeli, L. V. Schäfer, R. Linser, “Protein motional details revealed by complementary structural-biology techniques”, Structure (Cell Press), 28, 1-11, DOI: 10.1016/j.str.2020.06.001 (2020). (Link)

  57. J. Kotschy and R. Linser. “Proton-detected solid-state NMR and its applications to membrane proteins” in “Solid-State NMR: Applications in Biomembrane Structure, Eds. M.-A. Sani, F. Separovic, Institute of Physics (2020), DOI: 10.1088/978-0-7503-2532-5 (Link).

  58. H. Singh, C. K. Das S. K. Vasa, K. Grohe, L. V. Schäfer, R. Linser, “The active site of a prototypical “rigid” drug target is marked by extensive conformational dynamics”, Angew. Chem., Int. Ed., 59 (51), 22916-22921(2020), DOI: 10.1002/anie.202009348 (Link).

  59. R. Pallach, J. Keupp, K. Terlinden, L. Frentzel-Beyme, M. Kloß, A. Machalica, J. Kotschy, S. K. Vasa, P. A. Chater, C. Sternemann, M. T. Wharmby, R. Linser, R. Schmid, S. Henke, “Frustrated flexibility in metal-organic frameworks”, Nat. Commun., 4097 (2021), DOI: 10.1038/s41467-021-24188-4 (Link).

  60. A. Klein, P. Rovó, V. V. Sakhrani, Y. Wang, J. B. Holmes, V. Liu, P. Skowronek, L. Kukuk, S. K. Vasa, P. Güntert, L. J. Mueller, R. Linser, “Atomic-Resolution Chemical Characterization of (2x)72 kDa Tryptophan Synthase via 4D and 5D 1H-Detected Solid-State NMR”, Proc. Natl. Acad. Sci. U.S.A, (2022), DOI: 10.1073/pnas.2114690119 (Link).

  61. B. Buchmuller, J. Dröden, H. Singh, S. Palei, M. Drescher, R. Linser*, D. Summerer*, “Evolved DNA Duplex Readers for Strand-Asymmetrically Modified 5-Hydroxymethylcytosine/5-Methylcytosine CpG Dyads”, J. Am. Chem. Soc. , 144 (7), 2987–2993 (2022), DOI: 10.1021/jacs.1c10678 (Link).

  62. A. Klein, S. K. Vasa, B. Söldner, K. Grohe, R. Linser, “Unambiguous Sidechain Assignments for Solid-State Nuclear Magnetic Resonance Structure of Non-deuterated Proteins via a Combined 5D/4D Sidechain-to-Backbone Experiment”, J. Phys. Chem. Lett., 13, 1644–1651 (2022), DOI: 10.1021/acs.jpclett.1c04075 (Link).

  63. E. Burakova, S. K. Vasa, R. Linser, “Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR”, J. Biomol. NMR, 76, 197–212 (2022), DOI: 10.1007/s10858-022-00405-0 (Link).

  64. B. Söldner, K. Grohe, P. Neidig, J. Auch, S. Blach, A. Klein, S. K. Vasa, L. V. Schäfer, R. Linser, “Integrated Assessment of Structure and Dynamics of Solid Proteins”, J. Phys. Chem. Lett. 14, 1725−1731 (2023), DOI.: 10.1021/acs.jpclett.2c03398 (Link).

  65. H. Singh, C. K. Das, B. Buchmuller, L. Schäfer*, D. Summerer*, R. Linser*, “Epigenetic CpG Duplex Marks Probed by an Evolved DNA Reader via a Well-Tempered Conformational Plasticity“, Nucleic Acids Res., 51, 6495–6506 (2023), DOI: 10.1093/nar/gkad134 (Link). (Cover article: See the picture here!)

  66. A. Klein, S. K. Vasa, R. Linser, “5D solid-state NMR spectroscopy for facilitated resonance assignment“, J. Biomol. NMR, 77, 229–245 (2023), DOI: 10.1007/s10858-023-00424-5 (Link).

  67. J. Kotschy#, B. Söldner#, H. Singh, S. K. Vasa, R. Linser, “Microsecond Timescale Conformational Dynamics of a Small-Molecule Ligand within the Active Site of a Protein“, Angew. Chem., Int. Ed., 63 (5), e202313947 (2024), DOI:10.1002/anie.202313947 (Link). #: Equal contributions (Inside cover, see the picture here!)

  68. T.-C. Lin, L. Engelhard, B. Söldner, R. Linser, D. Summerer, “Light-Activatable MBD-Readers of 5-Methylcytosine Reveal Domain-Dependent Chromatin Association Kinetics In Vivo”, Adv. Sci., accepted (2023), DOI: 10.1002/advs.202307930 (Link).

  69. B. Kosel, K. Bigler, B. C. Buchmuller, S. R. Acharyya, R. Linser*, D. Summerer*, "Evolved Readers of 5-Carboxylcytosine CpG Dyads Reveal a High Versatility of the Methyl-CpG-Binding Domain for Recognition of Noncanonical Epigenetic Marks", Angew. Chem., Int. Ed., accepted (2024), DOI: 10.1002/anie.202318837. (Link)

  70. H. Aucharova#, A. Klein#, S. Medina Gomez, B. Söldner, S. K. Vasa, R. Linser, "Protein deuteration via algal amino acids to overcome proton back-exchange for fast-MAS solid-state NMR of large proteins", Chem. Commun., 60, 3083–3086 (2024), DOI: 10.1039/D4CC00213J. (Link) #: Equal contributions

  71. H. G. Daronkola#, B. Söldner#, H. Singh, R. Linser*, A. Vila Verde*, "Nonlinear impact of electrolyte solutions on protein dynamics", ChemBioChem, accepted (2024), DOI: 10.1002/cbic.202400057. (Link) #: Equal contributions

  72. W.-L. Xue, P. Kolodzeiski, H. Kavaleuskaya, S. K. Vasa, A. Koutsianos, R. Pallach, J. Song , L. Frentzel-Beyme, R. Linser, S. Henke, "Highly porous metal-organic framework liquids and glasses via a solvent-assisted linker exchange strategy of ZIF-8", Nat. Commun., accepted (2024).

  73. D. Bell, F. Lindemann, L. Gerland, H. Aucharova, A. Klein, D. Friedrich, M. Hiller, K. Grohe, B. van Rossum, A. Diehl, J. Hughes, L. J. Mueller, R. Linser, A.-F. Miller, H. Oschkinat, "Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR – practical aspects", J. Biomol. NMR, accepted (2024).



  1. S. Medina Gomez, I. Visco, F. Merino, P. Bieling, R. Linser, "Transient structural properties of the Rho GDP-dissociation inhibitor", major revisions for Angew. Chem., accessible in its originally submitted form on biorXiv.
  2. S. Medina Gomez, S. K. Vasa, R. Linser, "Allostery at a protein-protein interface harboring an intermolecular dynamic network", accessible in its current form on biorXiv.