ArticleBiophysical journal2007
Modeling a spin-labeled fusion peptide in a membrane: implications for the interpretation of EPR experiments.
Article in Biophysical journal, 2007. 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.
- Synthesis, Conformational Analysis and Antitumor Activity of the Naturally Occurring Antimicrobial Medium-Length Peptaibol Pentadecaibin and Spin-Labeled Analogs Thereof.International journal of molecular sciences · 2023Article
- Article
- Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion.International journal of molecular sciences · 2018Article
- High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.Journal of biomolecular NMR · 2017Article
- Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide.The journal of physical chemistry. B · 2015Article
- Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.Nature methods · 2013Article
- Identification and removal of nitroxide spin label contaminant: impact on PRE studies of α-helical membrane proteins in detergent.Protein science : a publication of the Protein Society · 2012Article
- Whole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxation.Journal of the American Chemical Society · 2011Article
- Helical hairpin structure of influenza hemagglutinin fusion peptide stabilized by charge-dipole interactions between the N-terminal amino group and the second helix.Journal of the American Chemical Society · 2011Article
- Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Journal of the American Chemical Society · 2011Article
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Authors and funding
2 authors.
Funding
Abstract
Site-directed spin-labeling and electron paramagnetic resonance are powerful tools for studying structure and conformational dynamics of proteins, especially in membranes. The position of the spin label is used as an indicator of the position of the site to which it is attached. The interpretation of these experiments is based on the assumptions that the spin label does not affect the peptide configuration and that it has a fixed orientation and distance with respect to the protein backbone. Here, the validity of these assumptions is examined through implicit membrane molecular dynamics simulations of the influenza hemagglutinin fusion peptide that has been labeled with methanethiosulfonate spin label. We find that the methanethiosulfonate spin label can occasionally induce peptide orientations that differ from those adopted by the wild-type peptide. Furthermore, the spin-label resides, on average, several Angstroms deeper in the membrane than the corresponding backbone C(alpha)-atom even at sites pointing toward the solvent. The nitroxide spin label exhibits flexibility and adopts various configurations depending on the surrounding residues.
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