Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin. - Wikidata - wikimedia - TriplyDB

Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin.

Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin.

http://www.wikidata.org/entity/Q30839725

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Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study Context mediates antimicrobial efficacy of kinocidin congener peptide RP-1 Membrane interactions and pore formation by the antimicrobial peptide protegrin.Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.Effects of arginine density on the membrane-bound structure of a cationic antimicrobial peptide from solid-state NMR.Arginine dynamics in a membrane-bound cationic beta-hairpin peptide from solid-state NMR.Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR.Trehalose-protected lipid membranes for determining membrane protein structure and insertion.Protein structure refinement using 13C alpha chemical shift tensors Determining the orientation of protegrin-1 in DLPC bilayers using an implicit solvent-membrane model.Acyl-substituted dermaseptin S4 derivatives with improved bactericidal properties, including on oral microflora 2D 1H-31P solid-state NMR studies of the dependence of inter-bilayer water dynamics on lipid headgroup structure and membrane peptides Comparative molecular dynamics simulation studies of protegrin-1 monomer and dimer in two different lipid bilayers Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy.Orientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy.Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Solid-state NMR investigation of the depth of insertion of protegrin-1 in lipid bilayers using paramagnetic Mn2+.Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic beta-sheet and alpha-helical potentials.Molecular dynamics simulations of three protegrin-type antimicrobial peptides: interplay between charges at the termini, β-sheet structure and amphiphilic interactions.Computational studies of protegrin antimicrobial peptides: a review.Orientation of a beta-hairpin antimicrobial peptide in lipid bilayers from two-dimensional dipolar chemical-shift correlation NMR.Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance.Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis.Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.Orientation Determination of Membrane-Disruptive Proteins Using Powder Samples and Rotational Diffusion: A Simple Solid-State NMR Approach.Structure of the antimicrobial beta-hairpin peptide protegrin-1 in a DLPC lipid bilayer investigated by molecular dynamics simulation NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide.Infectious Disease: Connecting Innate Immunity to Biocidal Polymers.A common landscape for membrane-active peptides.Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR.Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria.Activity and biophysical inhibition resistance of a novel synthetic lung surfactant containing Super-Mini-B DATK peptide.Mechanical properties that influence antimicrobial peptide activity in lipid membranes.Antimicrobial Peptides Share a Common Interaction Driven by Membrane Line Tension Reduction.Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers.Utilizing ESEEM spectroscopy to locate the position of specific regions of membrane-active peptides within model membranes Surfactant protein C peptides with salt-bridges ("ion-locks") promote high surfactant activities by mimicking the α-helix and membrane topography of the native protein

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P2860

Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin.

http://www.wikidata.org/entity/Q30839725

description

2002 nî lūn-bûn

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2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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Solid-state NMR investigations ...... imicrobial peptide, protegrin.

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Solid-state NMR investigations ...... imicrobial peptide, protegrin.

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Solid-state NMR investigations ...... imicrobial peptide, protegrin.

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Solid-state NMR investigations ...... imicrobial peptide, protegrin.

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Solid-state NMR investigations ...... imicrobial peptide, protegrin.

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Solid-state NMR investigations ...... imicrobial peptide, protegrin.

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