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• Helical distortion in tryptophan- and lysine-anchored membrane-spanning alpha-helices as a function of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines method. [Erratum to document cited in C

Helical distortion in tryptophan- and lysine-anchored membrane-spanning alpha-helices as a function of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines method. [Erratum to document cited in C

by Daily, Anna E.; Greathouse, Denise V.; Van der Wel, Patrick C. A.; Koeppe II, R. Erdman

The authors have revised and updated the 2H quadrupolar splitting values for the side chain of Ala9 in the KWALP23 peptide to 22.2 kHz, 14.7 kHz, and 4.7 kHz in DLPC, DMPC, and DOPC bilayer membranes, respectively, from the previous values in Table 2 on page 484. With the revised values for the Ala9 quadrupolar splittings, the earlier suggestion of a kink disappears from the geometric analysis of labeled alanines of KWALP23. [on SciFinder(R)]