Diffusive protein interactions in human versus bacterial cells

Autor: Sarah Leeb, Therese Sörensen, Fan Yang, Xin Mu, Mikael Oliveberg, Jens Danielsson

Publikováno v: Current Research in Structural Biology, Vol 2, Iss , Pp 68-78 (2020)

Random encounters between proteins in crowded cells are by no means passive, but found to be under selective control. This control enables proteome solubility, helps to optimise the diffusive search for interaction partners, and allows for adaptation

Externí odkaz: https://doaj.org/article/3acb138201b246a3805b50163ab91356

Transient Diffusive Interactions with a Protein Crowder Affect Aggregation Processes of Superoxide Dismutase 1 β-Barrel

Autor: Kenji Sugase, Masahiro Shirakawa, Daichi Morimoto, Erik Walinda, Sarah Leeb, Jens Danielsson, Naoto Iwakawa

Publikováno v: The Journal of Physical Chemistry B. 125:2521-2532

Aggregate formation of superoxide dismutase 1 (SOD1) inside motor neurons is known as a major factor in onset of amyotrophic lateral sclerosis. The thermodynamic stability of the SOD1 β-barrel has been shown to decrease in crowded environments such

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75c2d0f2cf8505f2c9298a17a3ff4028
https://doi.org/10.1021/acs.jpcb.0c11162

Diffusive protein interactions in human versus bacterial cells

Autor: Therese Sörensen, Xin Mu, Mikael Oliveberg, Sarah Leeb, Fan Yang, Jens Danielsson

Publikováno v: Current Research in Structural Biology, Vol 2, Iss, Pp 68-78 (2020)
Current Research in Structural Biology

Random encounters between proteins in crowded cells are by no means passive, but found to be under selective control. This control enables proteome solubility, helps to optimise the diffusive search for interaction partners, and allows for adaptation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a633e9a70abe133fa05a613e1179747
http://www.sciencedirect.com/science/article/pii/S2665928X20300064

Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry

Autor: Arthur Laganowsky, Kaare Teilum, Mikael Oliveberg, Justin L. P. Benesch, Rui M. M. Branca, Erik G. Marklund, Joana Costeira-Paulo, Mia L Abramsson, Mingming Xu, Lisa Lang, Michael Landreh, Leopold L. Ilag, Carol V. Robinson, Axel Leppert, Jonathan T. S. Hopper, Shane A. Chandler, Timothy M. Allison, Nicklas Österlund, Cagla Sahin, Jens Danielsson, Jakob R. Winther

Publikováno v: JACS Au
Abramsson, M L, Sahin, C, Hopper, J T S, Branca, R M M, Danielsson, J, Xu, M, Chandler, S A, Österlund, N, Ilag, L L, Leppert, A, Costeira-Paulo, J, Lang, L, Teilum, K, Laganowsky, A, Benesch, J L P, Oliveberg, M, Robinson, C V, Marklund, E G, Allison, T M, Winther, J R & Landreh, M 2021, ' Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry ', JACS Au, vol. 1, no. 12, pp. 2385-2393 . https://doi.org/10.1021/jacsau.1c00458
JACS Au, Vol 1, Iss 12, Pp 2385-2393 (2021)

In solution, the charge of a protein is intricately linked to its stability, but electrospray ionization distorts this connection, potentially limiting the ability of native mass spectrometry to inform about protein structure and dynamics. How the be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e5e9d258ed55683ae9250b0d910a94b

Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements

Autor: Sarah Leeb, Jens Danielsson

Publikováno v: Methods in Molecular Biology ISBN: 9781071605233

In the disordered state, a protein exhibits a high degree of structural freedom, in both space and time. For an ensemble of disordered or unfolded proteins, this means that the ensemble comprises a high diversity of structures, ranging from compact c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c91825e6b3da1611a2083091d1068200
https://doi.org/10.1007/978-1-0716-0524-0_14