Zobrazeno 1 - 10
of 357
pro vyhledávání: '"Helmut, Grubmüller"'
Autor:
Simon M. Lauer, Maren Reepmeyer, Ole Berendes, Dorota Klepacki, Jakob Gasse, Sara Gabrielli, Helmut Grubmüller, Lars V. Bock, Andor Krizsan, Rainer Nikolay, Christian M. T. Spahn, Ralf Hoffmann
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract Proline-rich antimicrobial peptides (PrAMPs) inhibit bacterial protein biosynthesis by binding to the polypeptide exit tunnel (PET) near the peptidyl transferase center. Api137, an optimized derivative of honeybee PrAMP apidaecin, inhibits p
Externí odkaz:
https://doaj.org/article/6067bc78e2dd47b68285bb91c3a91b6d
Autor:
Lars V. Bock, Helmut Grubmüller
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The rapid temperature drop during plunge-freezing affects the structural ensembles obtained by cryo-EM. To quantify the extent of perturbation, Bock and Grubmüller combined continuum calculations, MD simulations, and kinetic models.
Externí odkaz:
https://doaj.org/article/a6b6b8b56ca94c4685df80659654c19f
Autor:
Rita Padányi, Bianka Farkas, Hedvig Tordai, Bálint Kiss, Helmut Grubmüller, Naoto Soya, Gergely L. Lukács, Miklós Kellermayer, Tamás Hegedűs
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 2587-2599 (2022)
Cystic fibrosis (CF) is a frequent genetic disease in Caucasians that is caused by the deletion of F508 (ΔF508) in the nucleotide binding domain 1 (NBD1) of the CF transmembrane conductance regulator (CFTR). The ΔF508 compromises the folding energe
Externí odkaz:
https://doaj.org/article/f824232d22a54693a0c1dca0363f6c83
Autor:
Bertrand Beckert, Elodie C. Leroy, Shanmugapriya Sothiselvam, Lars V. Bock, Maxim S. Svetlov, Michael Graf, Stefan Arenz, Maha Abdelshahid, Britta Seip, Helmut Grubmüller, Alexander S. Mankin, C. Axel Innis, Nora Vázquez-Laslop, Daniel N. Wilson
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Macrolides and ketolides antibiotics selectively interfere with the translation of a specific subset of proteins. Here the authors show how the macrolide erythromycin and the ketolide telithromycin interplay with the nascent polypeptide chain to arre
Externí odkaz:
https://doaj.org/article/15117e74a84f4129bf14254d7d049216
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-7 (2021)
Proteins need to overcome energy barriers to induce intermediate steps in membrane fusion. Using lipid vesicles in which progression to hemifusion is arrested, the authors show that the metastable intermediate is enhanced by divalent cations and is c
Externí odkaz:
https://doaj.org/article/901cfa95a349420482eaf82f901e41d0
Autor:
Lars V. Bock, Neva Caliskan, Natalia Korniy, Frank Peske, Marina V. Rodnina, Helmut Grubmüller
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Programmed ribosomal frameshifting (PRF) is an alternative translation strategy that causes controlled slippage of the ribosome along the mRNA, changing the sequence of the synthesized protein. Here the authors provide a thermodynamic framework that
Externí odkaz:
https://doaj.org/article/227669040cf540618b30da976bf14062
Autor:
Yangang Pan, Emmi Pohjolainen, Philipp A. M. Schmidpeter, Andrea C. Vaiana, Crina M. Nimigean, Helmut Grubmüller, Simon Scheuring
Publikováno v:
Nat Struct Mol Biol
Cyclic nucleotide-gated ion channels are crucial in many physiological processes such as vision and pacemaking in the heart. SthK is a prokaryotic homolog with high sequence and structure similarities to hyperpolarization-activated and cyclic nucleot
Autor:
Maxim Igaev, Helmut Grubmüller
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 9, p e1008132 (2020)
Tubulin dimers associate longitudinally and laterally to form metastable microtubules (MTs). MT disassembly is preceded by subtle structural changes in tubulin fueled by GTP hydrolysis. These changes render the MT lattice unstable, but it is unclear
Externí odkaz:
https://doaj.org/article/848b40c7a85549d7b395b5a91992f65f
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Existing methods to extract structural information from single-molecule scattering measurements require large number of photons per image. Here the authors discuss a method to reconstruct the structure of a molecule from X-ray scattering data by usin
Externí odkaz:
https://doaj.org/article/79a8e2c92386433192ebfcd421baa768
Publikováno v:
eLife, Vol 8 (2019)
We present a correlation-driven molecular dynamics (CDMD) method for automated refinement of atomistic models into cryo-electron microscopy (cryo-EM) maps at resolutions ranging from near-atomic to subnanometer. It utilizes a chemically accurate forc
Externí odkaz:
https://doaj.org/article/3735e46796954e399da7a0236631fb4f