Protein-Strukturbiologie mit Kernmagnetresonanz-Spektroskopie (NMR)
Extraordinary advances occurred during the last few years in structural biology by nuclear magnetic resonance (NMR) spectroscopy. The precision and accuracy of solution structures by NMR improved dramatically and the upper range of molecular weights accessible to NMR structure determination is still increasing.
Once reasonable solution conditions are found, NMR structure determination is straight forward. Using nuclear spins in biomolecular structural studies has required exceptional efforts integrating chemical physics, instrumentation development, new algorithms, and labelling strategies.
NMR can provide a realistic, dynamic and/or time averaged view of a macromolecule ligand interface or, even, the transient intramolecular interfaces seen during protein folding not available by other methods. This is an advantage in probing the role of local entropic contributions to binding using relaxation methods, and in the dissection of localized weak contributions, as in the 'SAR (structure activity relationships) by NMR' approach.
Lecher J, Schwarz CKW, Stoldt M, Smits SHJ, Willbold D, Schmitt L
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Wittlich M, Koenig BW, Hoffmann S, Willbold D
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Stangler T, Mayr LM, Willbold D