Zobrazeno 1 - 10
of 13
pro vyhledávání: '"NMR Spectroscopy | Hot Paper"'
Autor:
Wolfgang Bermel, Eduard V. Bocharov, Vladislav Yu. Orekhov, Björn M. Burmann, Irena Matečko-Burmann, Panagiota S. Georgoulia, Dmitry M. Lesovoy, Tammo Diercks
Publikováno v:
Angewandte Chemie (International Ed. in English)
Dysregulation of post‐translational modifications (PTMs) like phosphorylation is often involved in disease. NMR may elucidate exact loci and time courses of PTMs at atomic resolution and near‐physiological conditions but requires signal assignmen
Autor:
Robert Hänsel-Hertsch, P. Broft, Volker Doetsch, Harald Schwalbe, Anna Wacker, Lukáš Trantírek, M. Krafcikova, Simon Dzatko
Publikováno v:
Angewandte Chemie (International Ed. in English)
We report here the in‐cell NMR‐spectroscopic observation of the binding of the cognate ligand 2′‐deoxyguanosine to the aptamer domain of the bacterial 2′‐deoxyguanosine‐sensing riboswitch in eukaryotic cells, namely Xenopus laevis oocyt
Autor:
Hendrik R. A. Jonker, Birgit Tiemann, Hans Bakker, Aleksandra Shcherbakova, Krishna Saxena, Harald Schwalbe
Publikováno v:
Angewandte Chemie (International Ed. in English)
Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR
Autor:
Claudiu T. Supuran, Letizia Barbieri, Alessio Nocentini, Matteo Cremonini, Enrico Luchinat, Lucia Banci
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie (International Ed. in English)
Angewandte Chemie (International Ed. in English)
Structure‐based drug development is often hampered by the lack of in vivo activity of promising compounds screened in vitro, due to low membrane permeability or poor intracellular binding selectivity. Herein, we show that ligand screening can be pe
Autor:
David Flores, Markus Zweckstetter, Adriana Savastano, Eckhard Mandelkow, Harindranath Kadavath, Jacek Biernat
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie (International Ed. in English)
Angewandte Chemie. International Edition, 60 (2)
Angewandte Chemie / International edition 60(2), 726-730 (2021). doi:10.1002/anie.202011157
Angewandte Chemie (International Ed. in English)
Angewandte Chemie. International Edition, 60 (2)
Angewandte Chemie / International edition 60(2), 726-730 (2021). doi:10.1002/anie.202011157
Cellular condensation of intrinsically disordered proteins (IDPs) through liquid–liquid phase separation (LLPS) allows dynamic compartmentalization and regulation of biological processes. The IDP tau, which promotes the assembly of microtubules and
Autor:
Christoph Rademacher, Peter H. Seeberger, Elena Shanina, Giulio Fittolani, Martina Delbianco, Mónica Guberman
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie
Angewandte Chemie (International Ed. in English)
Angewandte Chemie
Angewandte Chemie (International Ed. in English)
Protein–glycan interactions mediate important biological processes, including pathogen host invasion and cellular communication. Herein, we showcase an expedite approach that integrates automated glycan assembly (AGA) of 19F‐labeled probes and hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9666228701b83f55d9bf4c50a2231aac
Autor:
Peter Kiraly, Nicolas Kern, Mateusz P. Plesniak, Mathias Nilsson, David J. Procter, Gareth A. Morris, Ralph W. Adams
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (2), pp.666-669. ⟨10.1002/anie.202011642⟩
Angewandte Chemie (International Ed. in English)
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (2), pp.666-669. ⟨10.1002/anie.202011642⟩
Angewandte Chemie (International Ed. in English)
2D NMR is an immensely powerful structural tool but it is time‐consuming. Targeting individual chemical groups by selective excitation in a 1D experiment can give the information required far more quickly. A major problem, however, is that proton N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62ee3acef552b64e93347d05507d445b
https://hal.archives-ouvertes.fr/hal-03425427/file/anie.202011642.pdf
https://hal.archives-ouvertes.fr/hal-03425427/file/anie.202011642.pdf
Publikováno v:
Angewandte Chemie. International Edition, 59 (43)
Angewandte Chemie (International Ed. in English)
Angewandte Chemie (International Ed. in English)
Current biological research increasingly focusses on large human proteins and their complexes. Such proteins are difficult to study by NMR spectroscopy because they often can only be produced in higher eukaryotic expression systems, where deuteration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3aa53e5da7dd215145c9b113d6f44bd0
https://hdl.handle.net/20.500.11850/439157
https://hdl.handle.net/20.500.11850/439157
Autor:
Sven Brüschweiler, Robert Konrat, Julia Schörghuber, Darryl B. McConnell, Gerd Bader, Andreas Beier, Bernhard Wolkerstorfer, Leonhard Geist, Dirk Kessler, Harald Engelhardt, Moriz Mayer, Gerald Platzer, Julian E. Fuchs, Roman J. Lichtenecker
Publikováno v:
Angewandte Chemie (International Ed. in English)
While CH–π interactions with target proteins are crucial determinants for the affinity of arguably every drug molecule, no method exists to directly measure the strength of individual CH–π interactions in drug–protein complexes. Herein, we pr
Autor:
G. Matthias Ullmann, Monika Timmer, Antonella Di Savino, Anneloes Blok, Marcellus Ubbink, Thijmen La Haye, Johannes M. Foerster
Publikováno v:
Angewandte Chemie (International Edition), 59(51)
Angewandte Chemie (International Ed. in English)
Angewandte Chemie (International Ed. in English)
Electrostatic interactions can strongly increase the efficiency of protein complex formation. The charge distribution in redox proteins is often optimized to steer a redox partner to the electron transfer active binding site. To test whether the opti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de163e47deb14275b31240a4e90fef07
http://resolver.tudelft.nl/uuid:fa8249e5-8680-4b3e-a1e0-3d4505ccd268
http://resolver.tudelft.nl/uuid:fa8249e5-8680-4b3e-a1e0-3d4505ccd268