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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. Very recently, structural refinement involving new information, the anisotropies to hydrodynamic and magnetic susceptibility axes, provides an exceptional stimulation to a possible completely fresh approach to NMR structure determination, perhaps in some much larger macromolecules.

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.



Mirecka, EA, Shaykhalishahi, H, Gauhar, A, Akgul, S, Lecher, J, Willbold, D, Stoldt, M, Hoyer, W

Sequestration of a β-hairpin for control of α-synuclein aggregation.
Angew.Chem.Int.Ed.Engl. 53: 4227 (2014)


Lecher J, Schwarz CKW, Stoldt M, Smits SHJ, Willbold D, Schmitt L

RTX toxin transporters tether its substrate prior to secretion via the unique function of its N- terminal domain.
Structure 20, 1778-1787 (2012)


Schünke S, Stoldt M, Lecher J, Kaupp UB, Willbold D

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.
Proc. Natl. Acad. Sci. USA 108, 6121-6126 (2011)


Schwarten M, Stoldt M, Mohrlüder J, Willbold D

Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain.
Biochem. Biophys. Res. Comm. 395, 426-431 (2010)


Schünke S, Stoldt M, Novak K, Kaupp UB, Willbold D

Solution structure of the M.loti K1 channel cyclic nucleotide binding domain in complex with cAMP.
EMBO Rep. 10, 729-735 (2009)


Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D

NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles.
FEBS J. 276, 6560-75 (2009)


Schmidt H, Hoffmann S, Tran T, Stoldt M, Stangler T, Wiesehan K, Willbold D

Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes.
J. Mol. Biol. 365, 1517-1532 (2007)



Wittlich M, Koenig BW, Hoffmann S, Willbold D

Structural characterisation of the transmembrane and cytoplasmic domains of human CD4.
Biochim Biophys Acta 1768, 2949-60 (2007)


Hänel K, Stangler T, Stoldt M, Willbold D

Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains.
J. Biomed. Sci. 13, 281-293 (2006)


Engler A, Stangler T, Willbold D

Structure of human immunodeficiency virus type 1 Vpr (34-51) peptide in micelle containing aqueous solution.
Eur. J. Biochem. 269, 3264-3269 (2002)




Stangler T, Mayr LM, Willbold D

Solution structure of the GABAA receptor associated protein GABARAP: Implications for biological function and its regulation.
J. Biol. Chem. 277, 13363-13366 (2002)



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