ArticleJournal of the American Chemical Society2011
Whole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxation.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Global Dynamics of a Protein on the Surface of Anisotropic Lipid Nanoparticles Derived from Relaxation-Based NMR Spectroscopy.The journal of physical chemistry. B · 2022Article
- NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- Concurrent Identification and Characterization of Protein Structure and Continuous Internal Dynamics with REDCRAFT.Frontiers in molecular biosciences · 2022Article
- Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies.FEBS open bio · 2021Review
- Interaction of Huntingtin Exon-1 Peptides with Lipid-Based Micellar Nanoparticles Probed by Solution NMR and Q-Band Pulsed EPR.Journal of the American Chemical Society · 2018Article
- Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings.Journal of the American Chemical Society · 2018Article
- Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds.Microbial cell factories · 2016Article
- Atomic-level description of protein-lipid interactions using an accelerated membrane model.Biochimica et biophysica acta · 2016Review
- Article
- Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide.The journal of physical chemistry. B · 2015Article
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.Journal of the American Chemical Society · 2015Article
- Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding.Journal of biomolecular NMR · 2015Article
- The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.The Journal of biological chemistry · 2015Article
- Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Frontiers in molecular biosciences · 2015Article
- Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.The journal of physical chemistry. B · 2014Article
- Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles.Journal of biomolecular NMR · 2013Article
- The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.Biopolymers · 2013Review
- pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Biological membranes present a highly fluid environment, and integration of proteins within such membranes is itself highly dynamic: proteins diffuse laterally within the plane of the membrane and rotationally about the normal vector of this plane. We demonstrate that whole-body motions of proteins within a lipid bilayer can be determined from NMR (15)N relaxation rates collected for different-sized bicelles. The importance of membrane integration and interaction is particularly acute for proteins and peptides that function on the membrane itself, as is the case for pore-forming and fusion-inducing proteins. For the influenza hemagglutinin fusion peptide, which lies on the surface of membranes and catalyzes the fusion of membranes and vesicles, we found large-amplitude, rigid-body wobbling motions on the nanosecond time scale relative to the lipid bilayer. This behavior complements prior analyses where data were commonly interpreted in terms of a static oblique angle of insertion for the fusion peptide with respect to the membrane. Quantitative disentanglement of the relative motions of two interacting objects by systematic variation of the size of one is applicable to a wide range of systems beyond protein-membrane interactions.
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