ArticleChembiochem : a European journal of chemical biology2016
Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.
Article in Chembiochem : a European journal of chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- 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
- 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
- Wavelength-Selective Fluorescence of a Model Transmembrane Peptide: Constrained Dynamics of Interfacial Tryptophan Anchors.Journal of fluorescence · 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
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Transmembrane helices of integral membrane proteins often are flanked by interfacial aromatic residues that can serve as anchors to aid the stabilization of a tilted transmembrane orientation. Yet, physical factors that govern the orientation or dynamic averaging of individual transmembrane helices are not well understood and have not been adequately explained. Using solid-state (2) H NMR spectroscopy to examine lipid bilayer-incorporated model peptides of the GWALP23 (acetyl-GGALW(LA)6 LWLAGA-amide) family, we observed substantial unwinding at the terminals of several tilted helices spanning the membranes of DLPC, DMPC, or DOPC lipid bilayers. The fraying of helix ends might be vital for defining the dynamics and orientations of transmembrane helices in lipid bilayer membranes.
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