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Shuyan Xiao, Lei Yang and Fei Li The structure and assembly model of the third transmembrane domain of Slc11a1 in SDS micelles revealed by NMR study of the Leu-substituted peptide Journal of Peptide Science 18

Version of Record online: 3 NOV 2011 | DOI: 10.1002/psc.1414

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The NMR study reveals that TMD3 segment of Slc11a1 has a strong propensity to aggregate to form an α-helix bundle in the micelle state by Leu-zipper interaction. The simultaneous substitutions of L136A/L140A cause disassociation of the peptide assembly while maintaining its α-helical structure.

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