Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy.
about
Mechanical properties of lipid bilayers and regulation of mechanosensitive function: from biological to biomimetic channelsAlamethicin Supramolecular Organization in Lipid Membranes from 19F Solid-State NMR.Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situInsertion into lipid bilayer of truncated pHLIP®peptide.Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteinsImportance of residue 13 and the C-terminus for the structure and activity of the antimicrobial peptide aurein 2.2.Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.Lipid-controlled peptide topology and interactions in bilayers: structural insights into the synergistic enhancement of the antimicrobial activities of PGLa and magainin 2Charge distribution and imperfect amphipathicity affect pore formation by antimicrobial peptides.Observing a model ion channel gating action in model cell membranes in real time in situ: membrane potential change induced alamethicin orientation change.Dependence of Alamethicin Membrane Orientation on the Solution Concentration.Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations.Recent results in alamethicin research.On the design of supramolecular assemblies made of peptides and lipid bilayers.The SMART model: Soft Membranes Adapt and Respond, also Transiently, in the presence of antimicrobial peptides.Response of GWALP transmembrane peptides to changes in the tryptophan anchor positions.Conformation, self-aggregation, and membrane interaction of peptaibols as studied by pulsed electron double resonance spectroscopy.Histidine-rich designer peptides of the LAH4 family promote cell delivery of a multitude of cargo.Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous InsertionStructure of self-aggregated alamethicin in ePC membranes detected by pulsed electron-electron double resonance and electron spin echo envelope modulation spectroscopiesSolution synthesis, conformational analysis, and antimicrobial activity of three alamethicin F50/5 analogs bearing a trifluoroacetyl label.Synthesis and conformational properties of a TOAC doubly spin-labeled analog of the medium-length, membrane active peptaibiotic ampullosporin A as revealed by CD, fluorescence, and EPR spectroscopies.Alamethicin self-assembling in lipid membranes: concentration dependence from pulsed EPR of spin labels.Synergistic combination of alkylphosphocholines with peptaibols in targeting Leishmania infantum in vitro.Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.Structure Determination of Membrane Peptides and Proteins by Solid-State NMR
P2860
Q26864371-3331D3CF-48EE-4962-A598-FF6FA2AFB833Q31147408-551E2632-FA90-4135-887F-08BF09E68ECEQ33659392-01354129-25FE-465E-86E7-577EA3AFC734Q33749973-E4834A3C-574F-4D42-B463-3D1603500664Q33842111-9D657A3F-BBEE-4EA8-A335-7D6AFC4D23ECQ34001644-472CC6C6-B958-49AD-A09A-D40532BD690AQ34250487-C825EECD-DE83-45F3-8BA3-24891DC07583Q34456490-9A0CEC90-64D0-42E0-8523-3F5E172CAABFQ34688801-68D1133C-7BF5-4E79-945D-526B92C4CAF2Q35869840-485C6160-4E3A-4FF9-83CF-914C6083EB5AQ35893745-96579073-990D-4817-864B-A94B39F20DC7Q36733647-7CC581B1-7D8C-4C96-8193-79E9DD152EC6Q37377334-968DBD84-2953-4948-BB80-A984425A75D2Q37848284-497E9F9E-CC4D-4CB7-A887-D581B98F2FF5Q38107441-6AD9D18D-62B0-454F-B1AA-1DB911FFA0BDQ38218558-54437172-A002-4EB2-B21B-F660A5058909Q38293342-95DE7054-BDDB-4239-A9B1-6633F8E4B1CCQ38353952-E8244BA2-9052-44C9-AB5B-605857488E2EQ38566027-A839CE5E-344B-43B1-A51D-96C2DAF3A0B1Q40389854-1C291F93-1A13-4B40-B9FB-A29CBAC994C1Q41165287-C3B2F30A-85BB-4752-91AA-61F0805B8E44Q42633126-33827A31-D975-4B21-B393-170E394E1348Q45881924-FF04CF7D-4A4A-4CDF-A5D3-622C1D12831DQ47907234-AEAA6DE2-599A-4007-8000-032116075E77Q50016008-C1EEB2F1-F144-4CFC-B420-A74761665B70Q52598514-BD922236-EDD1-4D41-BED0-1DCFA05C3B07Q52691465-4C5522E1-7837-4482-84CD-0B464FAF80F1Q58005956-0AC2BD2D-D7B5-4223-85FA-7FD37D0FCD78
P2860
Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Structure and alignment of the ...... solid-state NMR spectroscopy.
@en
Structure and alignment of the ...... solid-state NMR spectroscopy.
@nl
type
label
Structure and alignment of the ...... solid-state NMR spectroscopy.
@en
Structure and alignment of the ...... solid-state NMR spectroscopy.
@nl
prefLabel
Structure and alignment of the ...... solid-state NMR spectroscopy.
@en
Structure and alignment of the ...... solid-state NMR spectroscopy.
@nl
P2093
P2860
P1433
P1476
Structure and alignment of the ...... solid-state NMR spectroscopy.
@en
P2093
Burkhard Bechinger
Evgeniy S Salnikov
Herdis Friedrich
Joe D J O'Neil
Philippe Bertani
Siegmund Reissmann
P2860
P304
P356
10.1529/BIOPHYSJ.108.136242
P407
P577
2009-01-01T00:00:00Z