Publications

75. S. Medina Gomez, S. K. Vasaa, R. Linser,
"Allostery at a protein-protein interface harboring an intermolecular dynamic network",
accepted in Angew. Chem., Int. Ed. (2024)

74. 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.

73. 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).

72. S. Medina Gomez, I. Visco, F. Merino, P. Bieling, R. Linser,
"Transient structural properties of the Rho GDP-dissociation inhibitor",
accepted in Angew. Chem., Int. Ed. (2024)

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

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., accepted (2024), DOI: 10.1039/D4CC00213J, still accessible in its original form on biorXiv. #: Equal contributions.

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.

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/anie.202318837.

67. Julia Kotschy#, Benedikt Söldner#, Himanshu Singh, Suresh 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.202319145. #: Equal contributions (Inside cover)

66. Alexander Klein, Suresh K. Vasa, R. Linser,
“5D solid-state NMR spectroscopy for facilitated resonance assignment“,
J. Biomol. NMR, accepted (2023), DOI: 10.1007/s10858-023-00424-5.

65. 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

64. 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. gkad134 (2023), DOI: 10.1093/nar/gkad134

63.* E. Burakova, S. K. Vasa, R. Linser,
“Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR”,
J. Biomol. NMR, accepted (2022).

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.

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.

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, 119 (4) e2114690119 (2022), DOI: 10.1073/pnas.2114690119

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

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

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

56. . 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).

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, 71–82, DOI: 10.1007/s10858-019-00291-z (2020).

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).
Cover article

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).
Cover article

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)
Cover article

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).

50. A. Klein, S. K. Vasa, R. Linser,
“Automated projection spectroscopy in solid-state NMR",
J. Biomol. NMR 72, 163-170 (2018).

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).

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 (2018).

47. P. Rovó, R. Linser,
“Microsecond timescale solid-state backbone dynamics: a combined NMR approach”,
ChemPhysChem, 19, 34–39 (2018).

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).

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).

44. P. Rovó, R. Linser,
“Microsecond timescale proton rotating-frame relaxation under magic angle spinning”,
J. Phys Chem. 121 (25), 6117–6130 (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).

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).

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).

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).

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).

38. R. Linser,
“Protons as sensitive reporters for molecular details.”,
in the research report of the Max Planck Society (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).

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).

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).

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).

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).

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).

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 Profile” article: ChemPhysChem, 16 (18), 3743 (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).

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).

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).

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).

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).

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).

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).

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)

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).

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),
Spotlights article: J. Am. Chem. Soc., 2014, 136 (32), 11197.

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).

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).

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).

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).

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.)

15. R. Linser,
“Backbone Assignment of Perdeuterated Proteins Using Long-Range H/C-Dipolar Transfers”,
J. Biomol. NMR 52 (2), 151–158 (2012).

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).

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).

12. 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);

 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);

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).

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.

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).

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).

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).

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).

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).

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).

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).

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).

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).