Course content this year has been selected to help provide a "kick start" to experimental set-up and acquisition at 1.0 GHz+, with a view to making the most of UHF-NMR. We hope that anyone wishing to hone their skills in data acquisition & analysis, generally, as well as prospective users of the 1.0 GHz spectrometer at HWB-NMR, will benefit!
The level of instruction is aimed at Year 2 & 3 PhD students & post-docs using biomolecular solution-state NMR in their research, but anyone with an interest is warmly invited to attend. An introduction to the UHF-NMR systems will be given at the outset, to whet the appetite. Exposure to basic NMR spectroscopy and hands-on experience up to 800 MHz is advantageous, though not mandatory. Here is the programme:
Thursday 17th November
09.45 - 10.15: Arrival & refreshments
10.15 - 10.30: Welcome & Introduction to NMR Basic Training
10.30 - 12.00: An introduction to the ultra-high field systems (Instructors: Dr Maxim Mayzel, Senior Applications Chemist & Dr Rainer Kuemmerle, Head of NMR Applications, at Bruker-Switzerland)
Our Bruker instructors will include demonstrations of experimental set-up with special consideration to the differences between set up at ultra-high field and lower field spectrometers, covering topics such as experiment selection, optimisation of pulses, shimming, and locking, in order to gain the maximum benefits from UHF spectrometers.
12.00 - 12.45: Lunch
12.45 - 14.15: Probing backbone dynamics of proteins using 15N relaxation methods (Instructor: Prof Christina Redfield)
This session will focus on the use of a variety of 15N relaxation methods to obtain residue-specific information about the backbone dynamics of both structured and intrinsically disordered proteins on a range of timescales (ps to ms). Methods for data collection, data processing and data analysis to obtain parameters characterising dynamic behaviour will be covered. Some of the ‘pitfalls’ that can be encountered in NMR relaxation studies and ways to get around these will be presented. The advantages and disadvantages of collecting relaxation data at ultra-high field and at multiple fields will be discussed. Finally, the use of molecular dynamics simulations to complement experimental NMR relaxation studies will be introduced.
14.15 - 15.45: The use of methyl TROSY experiments in studies of large molecular weight species (Instructor: Dr Chris Waudby)
The selective 13CH3 labelling of amino acid side-chains against a perdeuterated background, together with the introduction of methyl-TROSY NMR methods, has revolutionised the study of high-molecular weight molecules and complexes. This session will introduce the theoretical basis of the methyl TROSY effect, and discuss sample preparation, basic acquisition methods, and assignment strategies. We will then survey the wide range of experiments that are available for the characterisation of dynamics from sub-τc timescales to seconds, and close with a discussion of some recent case studies.
15.45 - 16.00: Refreshment break
16.00 - 17.30: Best practice in NMR data processing (Instructors: Prof Geerten Vuister)
Optimised data processing is essential for the most accurate interpretation of NMR data. This final session guides us through processing multi-dimensional NMR data, highlighting the steps involved, different functions that can be employed, and the results that can be obtained (good and bad). With spectra routinely being acquired using sparse sampling techniques, optimal processing of these data will be demonstrated, together with comparisons using various examples.
17.30 - 17.45: Closing remarks & departure