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Updated: Jul 21, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
Screening molecular associations with lipid membranes using natural abundance 13C cross-polarization magic-angle
David A Middleton1, Eleri Hughes, Jillian Madine
1Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, P.O. Box 88, Sackville Street, Manchester M60 1QD, United Kingdom. david.a.middleton@umist.ac.uk
Abstract:
We describe an NMR approach for detecting the interactions between phospholipid membranes and proteins, peptides, or small molecules. First, 1H-13C dipolar coupling profiles are obtained from hydrated lipid samples at natural isotope abundance using cross-polarization magic-angle spinning NMR methods. Principal component analysis of dipolar coupling profiles for synthetic lipid membranes in the presence of a range of biologically active additives reveals clusters that relate to different modes of interaction of the additives with the lipid bilayer. Finally, by representing profiles from multiple samples in the form of contour plots, it is possible to reveal statistically significant changes in dipolar couplings, which reflect perturbations in the lipid molecules at the membrane surface or within the hydrophobic interior.
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