Abstract
Spectral resolution represents a prerequisite for NMR based structural studies in multior fully labeled polypeptides such as membrane proteins, peptide ligands or protein aggregates. Recent applications in immobilized proteins [1–4] and a membrane protein aggregate [5] revealed that characteristic chemical shift information obtained in the liquid-state improves and expedites spectral assignment under MAS [6] conditions. In many cases, the observed NMR line width may limit applications in polypeptides and proteins of larger size. In this context, correlation experiments are desirable that maximize the spectral resolution without compromising the structural information contained in the spectra.
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Luca, S., Filippov, D.V., Angerstein, B., van der Marel, G.A., van Boom, J.H., Baldus, M. (2001). Multiple-quantum spectroscopy of fully labeled polypeptides under MAS: A statistical and experimental analysis. 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_4
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DOI: https://doi.org/10.1007/978-94-017-2579-8_4
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