Abstract
NMR spectroscopy is a well-established technique to determine the structure of peptides and small proteins in solution, also when bound to detergent micelles or phospholipid bicelles. The structure of the peptide alone is, however, not conveying the full picture, if the peptide is bound to a micelle, since it does not tell anything about the orientation of the peptide in the micelle. This article describes how to obtain that information together with information on peptide structure.
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Acknowledgments
This work was supported by the Villum Kann Rasmussen Foundation (BioNET) and the Danish Research Councils for Free and for Strategic Research (DanCARD, project number 09-067075). The NMR laboratory at Aalborg University is supported by the Obel, SparNord, and Carlsberg Foundations. Gd(DTPA-BMA) was a gift from the local hospital.
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Supplementary material is available electronically from the author’s university homepage:
http://www.en.bio.aau.dk/research/biotechnology/nmr-spectroscopy/mmib-supplementary
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Wimmer, R., Uggerhøj, L.E. (2017). Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR. In: Hansen, P. (eds) Antimicrobial Peptides. Methods in Molecular Biology, vol 1548. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6737-7_6
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DOI: https://doi.org/10.1007/978-1-4939-6737-7_6
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