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Structural biology

The Swedish NMR centre is an international, national and local research infrastructure that provides access to state-of-the-art NMR instrumentation for structural biology projects.

We offer access to specialist support and NMR spectrometers for solution NMR in the range between 700 MHz and 900 MHz. Our spectrometers are equipped with state-of-the-art probes for unsurpassed sensitivity, and have contributed to publications in multiple areas of research. The Swedish NMR centre comprise two nodes, one in Gothenburg and one in Umeå, together encompassing a facility within SciLifeLab.

Within the research area of structural biology, examples of scientific questions answered are


Solution structure

The solution structure of a protein/domain of a protein is easily solved given that there is a well-defined three-dimensional structure. Proteins which are only partly folded can be studied combining classic structure determination and relaxation measurements to gain insight in function.


Chemical Shift Perturbation (CSP)

CSP is a straightforward method to study the interaction of a protein with something present in solution. All kinds of interactions can be monitored – from interactions with small molecules to binding to a large molecular complex such as a photosystem.


Relaxation

The core of protein function often lies in the dynamic properties of a protein. The interactions in the cell, performing catalysis or transport ligands/ions is all feasible because the ability of the protein to adapt its conformation.


Backbone assignment

Both relaxation measurements and CSP measurements requires that the backbone of the protein is assigned. This requires 13C and 15N (and for larger proteins 2H) labelled material. The method for assigning the backbone atoms have been optimised in-house to also include monitoring of the progress during data recording as well on the fly analysis.


Fragment based screening (FBS)

FBS is a methodology to observe a mixture of small molecules, with or without the presence of  a protein or other macromolecule, to find molecules which interact with the protein. For any potential interaction hits, measurements can also be done in the reverse mode, observing the protein instead, not only verifying positive binding but also providing detailed information about the interaction surface by studying CSP, see above.


Cell-free protein expression

For proteins with special requirements for labelling or inherent properties (toxicity for example) that prohibits expression in vivo, we offer an in-house cell-free protein expression system.
 

Sample requirements are highly dependent on the scientific question, but for structure determination and relaxation measurements, requiring the highest sample concentration, a volume of ~150 µl with a concentration of 500-800 µM (corresponding to ~1 mg of protein for a 10 kD protein) is sufficient. CSP can be done with as little as 5% of the amount mentioned above (50 µg).

Please do not hesitate to contact the staff at SNC for further information. Information about user fees and application form for access can be found here.