News and Updates
We are happy to be supporting the NMR Bootcamp and Annual User symposium – 17th to the 18th of November at the University of Birmingham run by the Henry Wellcome Building for Nuclear Magnetic Resonance (HWB-NMR). If you are interested in learning how to make the most of ultra-high field bimolecular NMR make sure to register to attend and apply for the Connect NMR UK Training Mobility Grant!
The High-field NMR Facility at the University of Liverpool are hosting a Ligand Screening day on the 4th November 2022! The day will introduce ligand screen design, experiments controls and 15N labelled proteins for site-specific ligand binding information
The International Council on Magnetic Resonance in Biological Systems – Early Career Researcher (ICMRBS-ECR) forum have restarted their online seminar series! With the next seminar scheduled for the 9th November
In the near future, NMR facility managers and users of NMR facilities across the UK and the EU will be asked to complete online surveys to gather information about their facilities and experiences with remote access to NMR spectrometers during the pandemic. The results of the surveys will inform other work packages in the Remote-NMR project aimed at developing a common protocol for remote access to NMR.
If you are a PI who is interested in organising an NMR workshop for training researchers and would like support, please get in contact (Benjamin.email@example.com) and we would be happy to provide whatever support we can!
The Connect NMR UK Call for Training Mobility Grant of up to £600 for current PhD students, PDRAs, academics and facility staff based in a UK university, attending a workshop or visiting an NMR facility for training.
Next Deadline 31st of October 2022
The team at University College London examine co-translational protein folding by developing site-specific 19F-labelling of nascent polypeptide chains translation-arrested on ribosomes. The significant sensitivity gains from 19F-labelling (relative to 15N and methyl-13C labelling schemes) uniquely enable detection of multiple conformations of the nascent chain during biosynthesis on the ~2.4 MDa ribosome. Examination of 19F NMR spectra of different lengths of an immunoglobulin-like domain within a multi-domain protein provide ’snapshots’ of its biosynthesis, and the novel observation of two folding intermediates. A range of 19F NMR techniques, combined with MD simulations and cryo-EM, are then used to quantitatively examine the structures, thermodynamics, dynamics, and kinetics of co-translational folding. Together, the data describe a mechanism for how the ribosome alters the folding pathway of a nascent protein by selectively stabilizing partially folded conformations, with implications towards understanding intermediates in other biologically important co-translational processes.
Direct 1H detection in solid state NMR is an important method for analysis of wide range of substances, from small organic molecules in pharmaceuticals, to large protein structures in bioscience. However, 1H detection remains a consistent challenge for NMR scientists, the line broadening effects of dipolar coupled 1H nuclei can be reduced through increased magic-angle spinning frequencies and/or 1H decoupling. The team at the University of Warwick demonstrate the optimisation of 1H PMLG homonuclear decoupling at high spinning speeds giving rise to enhanced resolution in the 1D 1H spectrum, as well as in a 2D 15N-1H heteronuclear correlation for natural abundance solids using 1H detected CP-J coupling based refocussed INEPT MAS NMR experiment in order to enable through-bond correlation.