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- W2042497084 abstract "Membrane-spanning WALP peptides of general sequence acetyl-GWW(LA)nLWWA-amide, in which “n” may range from about 3 to 12, have been well characterized. A kink induced by a central proline residue in WALP19-P10 (acetyl-GWWLALALAP10ALALALWWA-ethanolamide) has also been characterized (see Biochemistry 48: 11883). It was furthermore observed that the 2H-quadrupolar splittings from labeled alanine side chains in WALP19-P10 were especially sensitive to Leu-to-Ala substitutions elsewhere in the sequence. In this work, we examined the consequences of Leu-to-Gly substitutions within the proline-containing WALP19-P10, from a perspective that Leu-to-Gly substitutions could reasonably be expected to produce larger consequences than Leu-to-Ala substitutions. Circular dichroism spectra indicate small reductions in helicity for Gly substitutions in WALP19-P10, with the mean residue ellipticity values being similar for Leu-to-Gly substitutions on either side of the proline. Using 2H-alanines as probes within the sequence, we have found from deuterium NMR spectroscopy of peptides incorporated within oriented lipid bilayer samples that the segment N-terminal to proline is generally more susceptible to Leu-to-Gly substitutions on both sides of the proline. In contrast, the C-terminal domain is largely unaffected by the glycine substitutions in either the N- or C-terminal segment. Substitutions near the C-terminus have little effect on either segment." @default.
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- W2042497084 date "2011-02-01" @default.
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- W2042497084 title "Influence of Glycine Substitutions on Designed Proline-Containing Transmembrane Peptides" @default.
- W2042497084 doi "https://doi.org/10.1016/j.bpj.2010.12.3655" @default.
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