ArticleThe Journal of biological chemistry2010
Charged or aromatic anchor residue dependence of transmembrane peptide tilt.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 65 citations in OpenAlex.
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- Comparing Interfacial Trp, Interfacial His and pH Dependence for the Anchoring of Tilted Transmembrane Helical Peptides.Biomolecules · 2020Article
- Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix.Biochimica et biophysica acta. Biomembranes · 2020Article
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double-Arginine-Containing Helical Peptides in Bilayer Membranes.Chembiochem : a European journal of chemical biology · 2019Article
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Transmembrane Helix Integrity versus Fraying To Expose Hydrogen Bonds at a Membrane-Water Interface.Biochemistry · 2019Article
- Actionable Activating Oncogenic ERBB2/HER2 Transmembrane and Juxtamembrane Domain Mutations.Cancer cell · 2018Article
- Wavelength-Selective Fluorescence of a Model Transmembrane Peptide: Constrained Dynamics of Interfacial Tryptophan Anchors.Journal of fluorescence · 2018Article
- Membrane-Induced p KJournal of chemical theory and computation · 2018Article
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues.Biophysical journal · 2018Article
- Membrane Bending Moduli of Coexisting Liquid Phases Containing Transmembrane Peptide.Biophysical journal · 2018Article
- Influence of glutamic acid residues and pH on the properties of transmembrane helices.Biochimica et biophysica acta. Biomembranes · 2017Article
- Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices.Biochemistry · 2016Article
- Impairment on the lateral mobility induced by structural changes underlies the functional deficiency of the lupus-associated polymorphism FcγRIIB-T232.The Journal of experimental medicine · 2016Article
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.The Journal of biological chemistry · 2016Article
- Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.Chembiochem : a European journal of chemical biology · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The membrane-spanning segments of integral membrane proteins often are flanked by aromatic or charged amino acid residues, which may "anchor" the transmembrane orientation. Single spanning transmembrane peptides such as those of the WALP family, acetyl-GWW(LA)(n)LWWA-amide, furthermore adopt a moderate average tilt within lipid bilayer membranes. To understand the anchor residue dependence of the tilt, we introduce Leu-Ala "spacers" between paired anchors and in some cases replace the outer tryptophans. The resulting peptides, acetyl-GX(2)ALW(LA)(6)LWLAX(22)A-amide, have Trp, Lys, Arg, or Gly in the two X positions. The apparent average orientations of the core helical sequences were determined in oriented phosphatidylcholine bilayer membranes of varying thickness using solid-state (2)H NMR spectroscopy. When X is Lys, Arg, or Gly, the direction of the tilt is essentially constant in different lipids and presumably is dictated by the tryptophans (Trp(5) and Trp(19)) that flank the inner helical core. The Leu-Ala spacers are no longer helical. The magnitude of the apparent helix tilt furthermore scales nicely with the bilayer thickness except when X is Trp. When X is Trp, the direction of tilt is less well defined in each phosphatidylcholine bilayer and varies up to 70° among 1,2-dioleoyl-sn-glycero-3-phosphocholine, 1,2-dimyristoyl-sn-glycero-3-phosphocholine, and 1,2-dilauroyl-sn-glycero-3-phosphocholine bilayer membranes. Indeed, the X = Trp case parallels earlier observations in which WALP family peptides having multiple Trp anchors show little dependence of the apparent tilt magnitude on bilayer thickness. The results shed new light on the interactions of arginine, lysine, tryptophan, and even glycine at lipid bilayer membrane interfaces.
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