Covers

		Linser, R.; Dasari, M.; Hiller, M.; Higman, V.; Fink, U.; Lopez del Amo, J.-M.; Markovic, S.; Handel, L.; Kessler, B.; Schmieder, P.; Oesterhelt, D.; Oschkinat, H.; Reif, B. "Proton detected solid-state NMR of fibrillar and membrane proteins", Angew. Chem., Int. Ed. 50, 4508–4512 (2011).

		Linser, R.; Gelev, V.; Hagn, F.; Hyberts, S. G.; Arthanari, H.; Wagner, G. "Selective methyl labeling of eukaryotic membrane proteins using cell-free expression", J. Am. Chem. Soc. 136, 11308–11310 (2014).

		Rovó, P.; Grohe, K.; Giller, K.; Becker, S.; Linser, R. "Proton Transverse Relaxation as a Sensitive Probe for Structure Determination in Solid Proteins", ChemPhysChem 16, 3743-3743 (2015).

		Kulminskaya, N.; Vasa, S. K.; Giller, K.; Becker, S.; Kwan, A.; Sunde, M.; Linser, R. "Access to side-chain carbon information in deuterated solids under fast MAS through non-rotor-synchronized mixing", Chem. Commun. 52, 268-271 (2016, back cover).

		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).

		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).

		Vasa, S. K.; Singh, H.; Grohe, K.; Linser, R., Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration. Angew. Chem., Int. Ed. Angew. Chem., Int. Ed., 58 (17), 5465, (2019).

		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, 7871 (2019).

		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., DOI: 10.1021/jacs.9b05311 (2019). (Link)

		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).

		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 (Link).

Flopped cover suggestions:

			Linser, R.; Salvi, N.; Briones, R.; Rovó, P.; de Groot, B. L.; Wagner, G. The membrane anchor of the transcriptional activator SREBP is characterized by intrinsic conformational flexibility. Proc. Natl. Acad. Sci. U.S.A., 112, 12390-12395 (2015).

			Vasa, S. K.; Rovó, P.; Linser, R. Protons as versatile reporters in solid-state NMR spectroscopy Acc. Chem. Res. (2018), DOI: 10.1021/acs.accounts.8b00055.

		Rovó, P.; Smith, C. A.; Gauto, D.; de Groot, B. L.; Schanda, P.; Linser, R., 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 (2019).

		P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, R. Linser, “Vasa, S. K.; Singh, H.; Grohe, K.; Linser, R., Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration. Angew. Chem., Int. Ed., DOI: 10.1002/anie.201811714 (2019).