ArticleBiophysical journal2006
Structure of tightly membrane-bound mastoparan-X, a G-protein-activating peptide, determined by solid-state NMR.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 81 citations in OpenAlex.
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- Bioactive Peptides and Proteins from Wasp Venoms.Biomolecules · 2022Review
- Article
- Article
- Peptidomic analysis of the venom of the solitary beeThe journal of venomous animals and toxins including tropical diseases · 2017Article
- Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.The journal of physical chemistry letters · 2016Article
- Review
- Membrane-active peptides: binding, translocation, and flux in lipid vesicles.Biochimica et biophysica acta · 2014Review
- High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion.Journal of the American Chemical Society · 2014Article
- Secondary structural analysis of proteins based on (13)C chemical shift assignments in unresolved solid-state NMR spectra enhanced by fragmented structure database.Journal of biomolecular NMR · 2013Article
- Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.Biophysical journal · 2012Article
- Simultaneous acquisition of PAR and PAIN spectra.Journal of biomolecular NMR · 2012Article
- Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.The journal of physical chemistry. B · 2011Article
- Selective acylation enhances membrane charge sensitivity of the antimicrobial peptide mastoparan-x.Biophysical journal · 2011Article
- Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.Journal of biomolecular NMR · 2010Article
- Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.Biochemistry · 2009Article
- Wasp mastoparans follow the same mechanism as the cell-penetrating peptide transportan 10.Biochemistry · 2009Article
- Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries.Journal of the American Chemical Society · 2008Article
- Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles.Biochemistry · 2008Article
- Solid-state 2H NMR spectroscopy of retinal proteins in aligned membranes.Biochimica et biophysica acta · 2007Review
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of mastoparan-X (MP-X), a G-protein activating peptide from wasp venom, in the state tightly bound to anionic phospholipid bilayers was determined by solid-state NMR spectroscopy. Carbon-13 and nitrogen-15 NMR signals of uniformly labeled MP-X were completely assigned by multidimensional intraresidue C-C, N-CalphaCbeta, and N-Calpha-C', and interresidue Calpha-CalphaCbeta, N-CalphaCbeta, and N-C'-Calpha correlation experiments. The backbone torsion angles were predicted from the chemical shifts of 13C', 13Calpha, 13Cbeta, and 15N signals with the aid of protein NMR database programs. In addition, two 13C-13C and three 13C-15N distances between backbone nuclei were precisely measured by rotational resonance and REDOR experiments, respectively. The backbone structure of MP-X was determined from the 26 dihedral angle restraints and five distances with an average root-mean-square deviation of 0.6 A. Peptide MP-X in the bilayer-bound state formed an amphiphilic alpha-helix for residues Trp3-Leu14 and adopted an extended conformation for Asn2. This membrane-bound conformation is discussed in relation to the peptide's activities to form pores in membranes and to activate G-proteins. This study demonstrates the power of multidimensional solid-state NMR of uniformly isotope-labeled molecules and distance measurements for determining the structures of peptides bound to lipid membranes.
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