Günter Bovermann
Max Planck Society
11 Papers
199 Citations
Günter Bovermann is an academic researcher from Max Planck Society. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Nuclear Overhauser effect. The author has an hindex of 6, co-authored 11 publications.
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Papers
A 1H-NMR study of the solution conformation of secretin. Resonance assignment and secondary structure.
TL;DR: The solution conformation of the 27 residue polypeptide hormone secretin has been investigated by 1H‐NMR spectroscopy under conditions where it adopts a fully ordered structure as judged by circular dichroismSpectroscopy, namely in an aqueous solution of 40% (v/v) trifluoroethanol.
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The 3D structure of a cyclosporin analogue in water is nearly identical to the cyclophilin-bound cyclosporin conformation
TL;DR: It is demonstrated unambiguously that the large structure change is induced primarily by the polar solvent rather than by complex formation with cyclophilin.
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Pulsed field gradient one‐dimensional NMR selective ROE and TOCSY experiments
Claudio Dalvit,Günter Bovermann +1 more
TL;DR: In this article, a pulsed field gradient one-dimensional NMR selective ROE (rotating frame NOE) experiment was designed and successfully tested and the resulting spectra are of high quality and devoid of artefacts.
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Argyrins, immunosuppressive cyclic peptides from myxobacteria. II. Structure elucidation and stereochemistry
Larissa Vollbrecht,Heinrich Steinmetz,Gerhard Höfle,Lukas Oberer,Grety Rihs,Günter Bovermann,Peter von Matt +6 more
TL;DR: The structures of argyrins A-H were elucidated by NMR spectroscopy, chemical degradation and X-ray analysis as cyclic octapeptides as well as with the antibiotics A21459 A and B, whose structures are revised with respect to 4'-methoxytryptophan.
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1H NMR studies of echistatin in solution. Sequential resonance assignments and secondary structure.
TL;DR: Two-dimensional 1H-NMR methods have been used to obtain complete proton resonance assignments for the 49-residue protein echistatin from the viper Echis carinatus, finding that the protein in solution contains only a small amount of regular secondary structure with four very short beta-strands.
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