Abstract
Structure determination of membrane-associated polypeptides presents one of the major challenges to solid state NMR spectroscopy. Many studies have been carried out so far using selective isotope labels, such as 2H, 13C, or 15N[1]. These NMR-reporters can be incorporated into the protein backbone or side chains, to reveal local structural parameters and to describe the dynamic properties of the membrane-embedded molecule. For example, an distance r can be measured between a pair of labels by means of dipolar recoupling MAS techniques such as rotational resonance or REDOR[2]. Alternatively, uniaxially oriented samples are used to determine the angle A of a labelled molecular segment with respect to the membrane normal N[3,4,5]. The latter approach relies on the orientation-dependent resonance frequency, which carries information about the anisotropie chemical shift tensor (13C, 15N), the dipolar coupling (1H-15N), or the quadrupolar interaction (2H)[6,7].
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Grage, S.L., Salgado, J., Dürr, U., Afonin, S., Glaser, R.W., Ulrich, A.S. (2001). Solid state 19F-NMR of biomembranes. In: Kiihne, S.R., de Groot, H.J.M. (eds) Perspectives on Solid State NMR in Biology. Focus on Structural Biology, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-2579-8_8
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DOI: https://doi.org/10.1007/978-94-017-2579-8_8
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