ArticleBiophysical journal2010
Order parameters of a transmembrane helix in a fluid bilayer: case study of a WALP peptide.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026Review
- Implicit model to capture electrostatic features of membrane environment.PLoS computational biology · 2024Article
- Alteration of Average Thickness of Lipid Bilayer by Membrane-Deforming Inclusions.Biomolecules · 2023Article
- A Diazirine-Modified Membrane Lipid to Study Peptide/Lipid Interactions - Chances and Challenges.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Solid-State NMR Investigations of the MHC II Transmembrane Domains: Topological Equilibria and Lipid Interactions.The Journal of membrane biology · 2019Article
- Structure, Topology, and Dynamics of Membrane-Inserted Polypeptides and Lipids by Solid-State NMR Spectroscopy: Investigations of the Transmembrane Domains of the DQ Beta-1 Subunit of the MHC II Receptor and of the COP I Protein p24.Frontiers in molecular biosciences · 2019Article
- Structural Characterization of the Amyloid Precursor Protein Transmembrane Domain and Its γ-Cleavage Site.ACS omega · 2017Article
- NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.Biophysical journal · 2016Article
- Enhanced Sampling of Coarse-Grained Transmembrane-Peptide Structure Formation from Hydrogen-Bond Replica Exchange.The Journal of membrane biology · 2015Article
- Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptides.The journal of physical chemistry. B · 2013Article
- Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.Biophysical journal · 2013Article
- Buried lysine, but not arginine, titrates and alters transmembrane helix tilt.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Properties of membrane-incorporated WALP peptides that are anchored on only one end.Biochemistry · 2012Article
- The Transmembrane Helix Tilt May Be Determined by the Balance between Precession Entropy and Lipid Perturbation.Journal of chemical theory and computation · 2012Article
- Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.Biophysical journal · 2012Article
- Comparative analysis of the orientation of transmembrane peptides using solid-state (2)H- and (15)N-NMR: mobility matters.European biophysics journal : EBJ · 2012Article
- Tyrosine replacing tryptophan as an anchor in GWALP peptides.Biochemistry · 2012Article
- On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamics.Biophysical journal · 2011Article
- Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain.Biophysical journal · 2011Article
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8 authors.
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Abstract
A new solid-state NMR-based strategy is established for the precise and efficient analysis of orientation and dynamics of transmembrane peptides in fluid bilayers. For this purpose, several dynamically averaged anisotropic constraints, including (13)C and (15)N chemical shift anisotropies and (13)C-(15)N dipolar couplings, were determined from two different triple-isotope-labeled WALP23 peptides ((2)H, (13)C, and (15)N) and combined with previously published quadrupolar splittings of the same peptide. Chemical shift anisotropy tensor orientations were determined with quantum chemistry. The complete set of experimental constraints was analyzed using a generalized, four-parameter dynamic model of the peptide motion, including tilt and rotation angle and two associated order parameters. A tilt angle of 21 degrees was determined for WALP23 in dimyristoylphosphatidylcholine, which is much larger than the tilt angle of 5.5 degrees previously determined from (2)H NMR experiments. This approach provided a realistic value for the tilt angle of WALP23 peptide in the presence of hydrophobic mismatch, and can be applied to any transmembrane helical peptide. The influence of the experimental data set on the solution space is discussed, as are potential sources of error.
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