Scrutinizing the protein hydration shell from molecular dynamics simulations against consensus small-angle scattering data

Autor: Johanna-Barbara Linse, Jochen S. Hub

Publikováno v: Communications Chemistry, Vol 6, Iss 1, Pp 1-10 (2023)

Abstract Biological macromolecules in solution are surrounded by a hydration shell, whose structure differs from the structure of bulk solvent. While the importance of the hydration shell for numerous biological functions is widely acknowledged, it r

Externí odkaz: https://doaj.org/article/b07563456bb5479b92a8b64aa85bac11

Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre

Autor: Petra Båth, Analia Banacore, Per Börjesson, Robert Bosman, Cecilia Wickstrand, Cecilia Safari, Robert Dods, Swagatha Ghosh, Peter Dahl, Giorgia Ortolani, Tinna Björg Ulfarsdottir, Greger Hammarin, María-José García Bonete, Adams Vallejos, Lucija Ostojić, Petra Edlund, Johanna-Barbara Linse, Rebecka Andersson, Eriko Nango, Shigeki Owada, Rie Tanaka, Kensuke Tono, Yasumasa Joti, Osamu Nureki, Fangjia Luo, Daniel James, Karol Nass, Philip J. M. Johnson, Gregor Knopp, Dmitry Ozerov, Claudio Cirelli, Christopher Milne, So Iwata, Gisela Brändén, Richard Neutze

Publikováno v: Acta Crystallographica Section D Structural Biology. 78:698-708

Serial crystallography is a rapidly growing method that can yield structural insights from microcrystals that were previously considered to be too small to be useful in conventional X-ray crystallography. Here, conditions for growing microcrystals of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb1f5a91eac8f35496a07f4ecfc7a445
https://doi.org/10.1107/s2059798322004144

Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein during translation regulation

Autor: Nele Merret Hollmann, Pravin Kumar Ankush Jagtap, Johanna-Barbara Linse, Philip Ullmann, Marco Payr, Brice Murciano, Bernd Simon, Jochen S. Hub, Janosch Hennig

RNA binding proteins (RBPs) often engage multiple RNA binding domains (RBDs) to increase target specificity and affinity. However, the complexity of target recognition of multiple RBDs remains largely unexplored. Here we use Upstream of N-Ras (Unr),

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::910c55350f919fc27939d43102895dbb
https://doi.org/10.1101/2022.11.26.518022

Structure and dynamics of the quaternary hunchback mRNA translation repression complex

Autor: Janosch Hennig, Pawel Masiewicz, Mikhail M. Savitski, Frank Gabel, Jochen S. Hub, Mandy Rettel, Bernd Simon, Brice Murciano, Jakub Macošek, Kathryn Perez, Miloš T. Ivanović, Inga Loedige, Sophie L. Winter, Pravin Kumar Ankush Jagtap, Jaelle Foot, Johanna-Barbara Linse, Karine Lapouge

Publikováno v: Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, 49 (15), pp.8866-8885. ⟨10.1093/nar/gkab635⟩
Nucleic Acids Research, 2021, 49 (15), pp.8866-8885. ⟨10.1093/nar/gkab635⟩
Nucleic acids research 49(15), 8866-8885 (2021). doi:10.1093/nar/gkab635

A key regulatory process during Drosophila development is the localized suppression of the hunchback mRNA translation at the posterior, which gives rise to a hunchback gradient governing the formation of the anterior-posterior body axis. This suppres

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81be314ab74e25227140230362f0d50e
https://pubmed.ncbi.nlm.nih.gov/34329466

Three- and four-site models for heavy water: SPC/E-HW, TIP3P-HW, and TIP4P/2005-HW

Autor: Johanna-Barbara Linse, Jochen S. Hub

Publikováno v: The Journal of Chemical Physics. 154:194501

Heavy water or deuterium oxide, D2O, is used as solvent in various biophysical and chemical experiments. To model such experiments with molecular dynamics simulations, effective pair potentials for heavy water are required that reproduce the well-kno

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05bb933f2b390cc8d1bddbc77f22cd1b
https://doi.org/10.1063/5.0050841