High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion - Wikidata - thesis-toulmin - TriplyDB

High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion

High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion

http://www.wikidata.org/entity/Q27681265

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Antimicrobial peptides in 2014 Role of phenylalanine and valine10 residues in the antimicrobial activity and cytotoxicity of piscidin-1 Cosolvent, ions, and temperature effects on the structural properties of Cecropin A-Magainin 2 hybrid peptide in solutions.Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.Simulations of Membrane-Disrupting Peptides II: AMP Piscidin 1 Favors Surface Defects over Pores Solid-state NMR and membrane proteins.A Practical Implicit Membrane Potential for NMR Structure Calculations of Membrane Proteins.A polyalanine peptide derived from polar fish with anti-infectious activities Piscidin-1-analogs with double L- and D-lysine residues exhibited different conformations in lipopolysaccharide but comparable anti-endotoxin activities Engineering monolayer poration for rapid exfoliation of microbial membranes.Computational studies of peptide-induced membrane pore formation.Influence of membrane composition on the binding and folding of a membrane lytic peptide from the non-enveloped flock house virus.Anti-inflammatory activities of cecropin A and its mechanism of action.Antimicrobial Peptides Share a Common Interaction Driven by Membrane Line Tension Reduction.Applications of NMR to membrane proteins.Nuclease activity gives an edge to host-defense peptide piscidin 3 over piscidin 1, rendering it more effective against persisters and biofilms.Dynamic Nuclear Polarization as an Enabling Technology for Solid State Nuclear Magnetic Resonance Spectroscopy.Solid-state NMR structures of integral membrane proteins.The Curvature Induction of Surface-Bound Antimicrobial Peptides Piscidin 1 and Piscidin 3 Varies with Lipid Chain Length.Folding a viral peptide in different membrane environments: pathway and sampling analyses.Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms Membrane Active Peptides and Their Biophysical Characterization

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P2860

High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion

http://www.wikidata.org/entity/Q27681265

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2014 nî lūn-bûn

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2014 թուականի Մարտին հրատարակուած գիտական յօդուած

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2014 թվականի մարտին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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High-Resolution Structures and ...... Kinking, and Bilayer Immersion

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High-Resolution Structures and ...... Kinking, and Bilayer Immersion

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High-Resolution Structures and ...... Kinking, and Bilayer Immersion

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Journal of the American Chemical Society

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High-resolution structures and ...... kinking, and bilayer immersion

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Alexander E Dao

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B Scott Perrin

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Caitlin M Burzynski

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Mukesh Sharma

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Myriam L Cotten

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Richard M Venable

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Richard W Pastor

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Riqiang Fu

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Robert M Hayden

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Stanley J Opella

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P2860

Canonical dynamics: Equilibrium phase-space distributions

MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain.

Structure of tightly membrane-bound mastoparan-X, a G-protein-activating peptide, determined by solid-state NMR

CHARMM: the biomolecular simulation program

Structure and mechanism of action of the antimicrobial peptide piscidin

Solution structure and cell selectivity of piscidin 1 and its analogues

Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles

Structure and Dynamics of the Membrane-Bound Form of Pf1 Coat Protein: Implications of Structural Rearrangement for Virus Assembly

Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer

A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments

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3491-3504

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136

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Eduard Y. Chekmenev

Christopher V Grant

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2014-01-22T00:00:00Z

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