Changes in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations

Vitaly V. Vostrikov, Benjamin A. Hall, Denise V. Greathouse, Roger E. Koeppe, Mark S.P. Sansom

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

Abstract

Independent experimental and computational approaches show agreement concerning arginine/membrane interactions when a single arginine is introduced at selected positions within the membrane-spanning region of acetyl-GGALW 5LALALAL12AL14ALALW19LAGA- ethanolamide, designated GWALP23. Peptide sequence isomers having Arg in position 12 or position 14 display markedly different behaviors, as deduced by both solid-state NMR experiments and coarse-grained molecular dynamics (CG-MD) simulations. With respect to the membrane normal of DOPC or DPPC lipid bilayer membranes, GWALP23-R14 shows one major state whose apparent average tilt is ∼10° greater than that of GWALP23. The presence of R14 furthermore induces bilayer thinning and peptide displacement to "lift" the charged guanidinium toward the bilayer surface. By contrast, GWALP23-R12 exhibits multiple states that are in slow exchange on the NMR time scale, with CG-MD simulations indicating two distinct positions with different screw rotation angles in the membrane, along with an increased tendency to exit the lipid bilayer.

Original languageEnglish (US)
Pages (from-to)5803-5811
Number of pages9
JournalJournal of the American Chemical Society
Volume132
Issue number16
DOIs
StatePublished - Apr 28 2010

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