The NMR instruments available at the Bijvoet Centre are state-of-the-art Bruker spectrometers, suitable for all the standard pulse sequences. Tailored pulse sequences for structural determination of high molecular weight proteins and other dedicated applications are developed and available.
The Bijvoet Center at UU offers access and support for solution NMR studies of biomolecules at field strengths ranging from 600 to 950 MHz. The instruments are well-equipped for all standard structural and dynamical characterization of proteins or other biomolecules, with cryoprobes for enhanced sensitivity on three machines (600, 900, and 950 MHz). A dedicated Argon-laser setup is available on a 500 MHz spectrometer for light-sensitive experiments.
The Facility has extensive expertise in the study of protein structure, dynamics and interactions. Applications involving high molecular weight proteins or protein complexes, such as nucleosome-protein complexes (200-250 kDa) for instance, benefit from the available tailored pulse sequences, provided these samples are appropiately isotope-labelled. We can now also offer dedicated support for applications involving interactions of intrinsically disordered proteins.
For more information, please visit the website of the SONNMRLSF facility at the Bijvoet Centre.
For iNEXT-Discovery applications
Scientific background, significance and objectives
Please describe the general scientific background for your project, explain - to a non-expert in the biology of the system - why these questions are important, and clearly at the end define your objectives, in terms of the tangible results you want to obtain and the questions these results will help to address.
Project background in your lab & recent results
Please describe if preliminary 1D 1H NMR spectra or 2D 1H-15N-HSQC spectra have been already acquired on your target samples. Describe if you have already performed a screen for conditions, such as buffer optimization, that promote stability (with respect to slow precipitation) or better quality NMR spectra. Please provide the NMR sample molecular weight and the concentration that you are able to reach without precipitation. Possibly, a priori knowledge of the oligomerization state of the system is critical to sample labeling choice. Please provide preliminary information about oligomerization state of your system, if you have it.
Research required, requested
Please describe what are the exact questions that you need to answer. This will allow us to determine a list of the NMR experiments needed in order to characterize your system. To get structural information on proteins by solution NMR, isotopically labelled samples, usually 15N and/or 15N/13C, are required. For proteins with MW > 20 kDa, protein 2H labelling (partial or complete depending on the MW) is also needed. If you are unsure of the optimal method to address your question, please state this openly and use this space to explain as well as possible what are the exact questions that you need to answer; this will not affect your proposal negatively as part of our mission is to suggest the best experiment(s) for answering user questions.
Benefit for health, food, biotechnology or biomaterials
Please include a statement for the immediate or longer-term impact that your research might have in innovations related to the fields above. These do not need to lead to a “product” but to scientific or technical innovations that can be of value for translational research in any of the sectors above.