Transmembrane NMR structure

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Science  04 Apr 1997:
Vol. 276, Issue 5309, pp. 9
DOI: 10.1126/science.276.5309.9l

Nuclear magnetic resonance (NMR) methods have been used by MacKenzie et al. (p. 131) to determine the structure of the transmembrane domain of the protein glycophorin A. This 40-residue peptide was solubilized in aqueous detergent micelles. The monomers form α helices despite the large number of amino acids with a low propensity for helix formation, and the interface between the monomers is stabilized not by hydrogen bonding but by van der Waals interactions.

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