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The EMBO Journal|October 8, 1997
Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domainM McCoy, E S Stavridi, J L Waterman, et al.The Journal of Peptide Research : Official Journal of the American Peptide Society|May 12, 2005
Peptides and the development of double- and triple-resonance solid-state NMR of aligned samplesN Sinha, C V Grant, K S Rotondi, et al.Biochemistry|July 1, 1999
Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopyY Hashimoto, K Toma, J Nishikido, et al.Methods in Enzymology|April 6, 2005
NMR experiments on aligned samples of membrane proteinsA A De Angelis, D H Jones, C V Grant, et al.Journal of Biomolecular NMR|July 1, 1991
Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopyB Bechinger, Y Kim, L E Chirlian, et al.Pageof 8