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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.

Artikel 1

Strukturgalerie

c39


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)

3ZUA

cnbd_apo

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)

2KXL

atg8

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)

2KQ7

cnbd_camp

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)

2K0G

vpu

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)

2K7Y

sh3

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)

2OI3

2OJ2

cd4

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)

2KLU

x4

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)

1YO4

vpr

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)

1KZV

1KZT

1KZS

gabarap

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)

1KOT




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