Sam joins our group again for his PhD project! After having spent his masters project with us, he now comes back sponsored by the SOFI2 CDT. Sam will develop methods leveraging on convolutional neural networks to study protein conformational spaces. While currently Sam can only join us in an unusual “virtual” way, he is already at work. Looking forward to welcoming him in Durham, hopefully soon!
In this period of lock down caused by COVID-19, children are home schooled. We have joined the “Scientist Next Door ” project, organised by scientists from the university of Edinburgh and Durham, to share our excitement for science with them!
We hope to hold group video calls with families and discuss things we find interesting, share ideas and resources. And, as Scientists Next Door, after the lockdown is over, it would be great to meet in person!
If you are a scientist, consider joining too. If you are parent, get in touch! www.scientist-next-door.org
Eager to learn about how mass spectrometry can help structural biology? Join us in Bordeaux on the 5-7 October 2020 to learn everything about top-down and native MS, ion mobility, HDX, cross-linking and, of course, integrative modelling!
This week two Masters students joined our group. George, from Chemistry department, will work on expanding JabberDock capabilities while Holly, from Physics, will study protein conformational spaces via deep learning. Welcome both!
Today the group moves to Durham University Department of Physics, where Matteo will take the position of Assistant Professor in Condensed Matter Physics!
We are very excited to present JabberDock, our new protein-protein docking algorithm. JabberDock is capable of accommodating for rearrangements upon binding including side chain reorientations and backbone flexibility. To do this, it leverages Spatial and Temporal Intensity (STID) maps, our single volumetric representation for proteins surface, electrostatics and local dynamics. JabberDock is freely available on Github, and is presented in the following article:
Today we welcome Lorenza Pacini, PhD student in ENS Lyon under the supervision of Dr. Claire Lesieur and Prof. Laurent Vuillon (Université Savoie Mont Blanc). Lorenza will spend one month with us, developing methods to model protein fibrils. Looking forward to some collaborative software development!
Sam successfully completed his Masters project with us, presenting a great poster on his study of peptide-lipid interactions by molecular dynamics simulations. Congratulations!
Small Heat Shock proteins such as HspB1 are molecular chaperones in charge of preventing harmful misfolding of proteins under stress conditions. Work led by the Benesch and Gehmlich groups shows, from muscle fibers down to single molecules, that phosphorylation of HspB1 alters its intramolecular dynamics, facilitating its binding to the mechanosensitive Filamin C. In good correspondence with NMR data, our calculations reveal that over over the course of microsecond-long simulations the N-terminus of HspB1 detaches from the rest of the protein.
Collier M.T., Alderson, T.R., de Villiers, C.P., Nicholls, D. , Gastall, H.Y., Allison, T.M., Degiacomi M.T., Jiang, H., Mlynek, G., Fürst, D.O., van der Ven, P.F.M., Djinovic-Carugo, K., Baldwin, A.J., Watkins, H., Gehmlich, K., Benesch, J.L.P. (2019), HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C. Science Advances, 5(5)
The image shows the structure of the long-lived small heat-shock proteins (present in the eye lens), and the effect of age-related isomerisation of key amino-acids, as detailed in our article.
[image composed with Gimp from protein VMD rendering redesigned by the artistic hand of Valentina Erastova]