Impact of 5-formylcytosine on the melting kinetics of DNA by 1H NMR chemical exchange Romeo C. A. Dubini, Alexander Schön, Markus Müller, Thomas Carell, and Petra Rovó Nucleic Acids Research 2020, accepted manuscript

doi: PDF

Rational Design of Covalent Cobaloxime-COF Hybrids for Enhanced Photocatalytic Hydrogen Evolution Kerstin Gottschling, Gökcen Savasci, Hugo A. Vignolo-González, Sandra Schmidt, Philipp Mauker, Tanmay Banerjee, Petra Rovó, Christian Ochsenfeld, and Bettina Lotsch J. Am. Chem. Soc. 2020, accepted manuscript


Protein motional details revealed by complementary structural-biology techniques Kristof Grohe, Snehal Patel, Cornelia Hebrank, Sara Medina, Alexander Klein, Petra Rovó Suresh K. Vasa, Himanshu Singh, Beat Vögeli, Lars V. Schäfer, and Rasmus Linser Structure 2020, accepted manuscript


Recent advances in solid-state relaxation dispersion techniques Petra Rovó Solid State Nuclear Magnetic Resonance 2020, 108, 101665

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Fast Microsecond Dynamics of the Protein-Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy Himanshu Singh, Suresh K. Vasa, Harish Jangra, Petra Rovó, Christopher Päslack, Chandan K. Das, Hendrik Zipse, Lars V. Schäfer, and Rasmus Linser ; J. Am. Chem. Soc. 2019, 141, (49), 19276-19288.

doi: PDF

proto‐Urea‐RNA (Wöhler RNA) containing unusually stable urea nucleosides Hidenori Okamura, Antony Crisp, Sarah Hübner, Sidney Becker, Petra Rovó, Thomas Carell; Angew Chem Int Ed 2019

doi: 10.1002/anie.201911746

Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques Petra Rovó, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda, and Rasmus Linser; J. Am. Chem. Soc. 2019, 141, (2), 858-869.

doi: 10.1021/jacs.8b09258 PDF


Protons as versatile reporters in solid-state NMR spectroscopy Suresh K. Vasa, Petra Rovó and Rasmus Linser; Acc. Chem. Res. 2018, 51, 1386–1395

doi: 10.1021/acs.accounts.8b00055 PDF

Dynamics and interactions of a 29 kDa human enzyme studied by solid-State NMR Suresh K. Vasa, Himanshu Singh, Petra Rovó and Rasmus Linser; J. Phys. Chem. Lett., 2018, 9 (6), 1307-1311.

doi: 10.1021/acs.jpclett.8b00110 PDF

Microsecond timescale protein dynamics: a combined solid‐State NMR approach Petra Rovó and Rasmus Linser; ChemPhysChem 2018, 19 (1), 34-39.

doi: 10.1002/cphc.201701238 PDF


Microsecond timescale proton rotating-frame relaxation under magic angle spinning Petra Rovó and Rasmus Linser, J. Phys. Chem. B, 2017, 121, 6117-6130.

doi: 10.1021/acs.jpcb.7b03333

Four faces of the interaction between ions and aromatic rings Dóra Papp, Petra Rovó, Imre Jákli, Attila G. Császár and András Perczel, J. Comput. Chem., 2017, 38, 1762-1773.

doi: 10.1002/jcc.24816

Protein conformational dynamics studied by 15N and 1H R1r relaxation dispersion: Application to wild-type and G53A ubiquitin crystals Diego F. Gauto, Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser and Paul Schanda, Solid State Nucl. Magn. Res., 2017, 86, 87-95.

doi: 10.1016/j.ssnmr.2017.04.002


Access to aliphatic protons as reporters in non-deuterated proteins by ssNMR Suresh K. Vasa, Petra Rovó, Karin Giller, Stefan Becker and Rasmus Linser, PhysChemChemPhys, 2016, 18, 8359-8363.

doi: 10.1039/c5cp06601h


Proton Transverse Relaxation as a Sensitive Probe for Structure Determination in Solid Proteins Petra Rovó, Kristof Grohe, Karin Giller, Stefan Becker and Rasmus Linser, ChemPhysChem, 2015, 16, 3791-3796.

doi: 10.1002/cphc.201500799

The membrane anchor of the transcriptional activator SREBP is characterized by intrinsic conformational flexibility Rasmus Linser, Nicola Salvi, Rodolf Briones, Petra Rovó, Bert L. de Groot and Rasmus Linser Proc Natl Acad Sci U S A 2015, 112, 19390- 19395.

doi: 10.1073/pnas.1513782112 PDF

Sequential backbone assignment based on dipolar amide-to-amide correlation experiments, Shengqi Xiang, Kristof Grohe, Petra Rovó, Suresh K. Vasa, Karin Giller, Stefan Becker and Rasmus Linser, J. Biomol. NMR, 2015, 62, 303-311.

doi: 10.1007/s10858-015-9945-4

Phosphorylation as conformational switch to amyloid state: Trp-cage as protein aggregation model József Kardos, Bence Kiss, András Micsonai, Petra Rovó, Dóra K. Menyhárd, János Kovács, Györgyi Váradi, Gábor K. Tóth and András Perczel, J. Phys. Chem. B, 2015, 191, 2946-2955.

doi: 10.1021/jp5124234


Rational design of alpha-helix stabilized Exendin-4 analogues, Petra Rovó, Viktor Farkas, Pál Stráner, Mária Szabó, Ágnes Jermendy, Orsolya Hegyi, Gábor K. Tóth and András Perczel, Biochemistry, 2014, 53, 3540-3545.

doi: 10.1021/bi500033c


Structural Insights into the Trp-Cage Folding Intermediate Formation, Petra Rovó, Pál Stráner, András Láng, István Bartha, Kristóf Huszár, László Nyitray and András Perczel, Chem. Eur. J., 2013, 19, 2628-2640.

doi: 10.1002/chem.201203764


Cooperativity network of Trp-cage miniproteins: Probing salt-bridges, Petra Rovó, Viktor Farkas, Orsolya Hegyi, Orsolya Csikós, Gábor Tóth and András Perczel, J. Peptid Sci., 2011, 17, 610-619.

doi: 10.1002/psc.1377

Signologs: Orthology-Based Identification of Novel Signaling Pathway Components in Three Metazoans, Tamás Korcsmáros, Máté S. Szalay, Petra Rovó, Robin Palotai, Dávid Fazekas, Katalin Lenti, Illés J. Farkas, Péter Csermely and Tibor Vellai, PLoS ONE, 2011, 6 e19240

doi: 10.1371/journal.pone.0019240


Uniformly curated signaling pathways reveal tissue-specific cross-talks and drug target candidates, Tamás Korcsmáros, Illés J. Farkas, Máté S. Szalay, Petra Rovó, Dávid Fazekas, Zoltán Spiró, Csaba Böde, Katalin Lenti, Tibor Vellai and Péter Csermely, Bioinformatics, 2010, 26, 2042-2050.

doi: 10.1093/bioinformatics/btq310