Zobrazeno 1 - 10
of 113
pro vyhledávání: '"Beat, Vögeli"'
Autor:
Dzmitry Ashkinadze, Harindranath Kadavath, Aditya Pokharna, Celestine N. Chi, Michael Friedmann, Dean Strotz, Pratibha Kumari, Martina Minges, Riccardo Cadalbert, Stefan Königl, Peter Güntert, Beat Vögeli, Roland Riek
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
In this manuscript the authors report accurate multi-state protein structures of the PDZ domain using biological NMR. By looking into protein structural states, the authors report an allosteric pathway at atomic resolution that validates previously r
Externí odkaz:
https://doaj.org/article/6b3bc663eccc4bfea2bb66b7062c25de
Autor:
Ju-Sim Kim, Alexandra Born, James Karl A. Till, Lin Liu, Sashi Kant, Morkos A. Henen, Beat Vögeli, Andrés Vázquez-Torres
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
The response regulator SsrB, a master activator of the Salmonella pathogenicity island-2 gene cluster, is under allosteric control of thioredoxin. Authors utilise in vitro and in vivo models to investigate if other members of the response regulator f
Externí odkaz:
https://doaj.org/article/0efe26c693194b90b5cbf85edd28c641
Autor:
Alexandra Born, Janne Soetbeer, Morkos A. Henen, Frauke Breitgoff, Yevhen Polyhach, Gunnar Jeschke, Beat Vögeli
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-9 (2022)
Born et al. describe interdomain allostery in the two domain peptidyl-prolyl isomerase Pin1 upon binding of two ligands. These ligands couple population shifts of extended and compact states to changes in the catalytic site of Pin1.
Externí odkaz:
https://doaj.org/article/9444f470131e41d4b1a5ac4920e3a5e4
On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins
Publikováno v:
Magnetic Resonance Letters, Vol 2, Iss 2, Pp 61-68 (2022)
Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic fie
Externí odkaz:
https://doaj.org/article/a53558b5d6784be7aae1350403da9d49
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/10377cc98cea457a86b8741fbfdcf201
Publikováno v:
Magnetochemistry, Vol 9, Iss 7, p 166 (2023)
Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adap
Externí odkaz:
https://doaj.org/article/ea0e34622404486887191c50a7925d88
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
ADAR1 is an interferon-induced enzyme that catalyzes editing of adenine to inosine across the transcriptome as part of the immune response. Here the authors establish how ADAR1 recognizes non-CpG RNA sequences to facilitate the formation of A-Z junct
Externí odkaz:
https://doaj.org/article/75d14e461d4e48f38695886425928e67
Publikováno v:
Magnetochemistry, Vol 9, Iss 1, p 33 (2023)
Protein methyl groups can participate in multiple motional modes on different time scales. Sub-nanosecond to nano-second time scale motions of methyl axes are particularly challenging to detect for small proteins in solutions. In this work we employ
Externí odkaz:
https://doaj.org/article/f94c805ab4b641e495120d4e21764be8
Publikováno v:
Molecules, Vol 28, Iss 2, p 843 (2023)
Despite structural differences between the right-handed conformations of A-RNA and B-DNA, both nucleic acids adopt very similar, left-handed Z-conformations. In contrast to their structural similarities and sequence preferences, RNA and DNA exhibit d
Externí odkaz:
https://doaj.org/article/43bf6fe3323f483abeee199be5a8d287
Publikováno v:
Biomolecular NMR Assignments. 17:151-157
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef528e61b195408c7db5436135891fc2
https://doi.org/10.1007/s12104-023-10134-6
https://doi.org/10.1007/s12104-023-10134-6