About: The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes

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About: The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes Goto Sponge NotDistinct Permalink

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scientific article published on 01 June 1988

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 1988 (uk) artículu científicu espublizáu en xunu de 1988 (ast) scientific article published on 01 June 1988 (en) im Juni 1988 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q69041233-D8282F6A-A66B-47EF-9941-CF15F71CFEC0
publication date	1988-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q69041233-76159B84-EBB0-430E-9419-6529545D50C7
language of work or name	English
author name string	wds:Q69041233-0D37E86D-03DB-47BA-AF3E-4A49A2D71049 wds:Q69041233-3CF2A11E-F64D-4321-ACFE-C90AEE58C3CC wds:Q69041233-480249E6-9482-45B2-8FB2-40855A6B66AC wds:Q69041233-4CCC25A0-6F9C-4C2E-8D6D-1894FF482EA6
author name string	J A Killian D W Urry K U Prasad D Hains
rdfs:label	The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (en) The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (nl)
skos:prefLabel	The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (en) The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (nl)
name	The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (en) The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (nl)
title	wds:Q69041233-43006076-AAE0-484A-9A69-E3C32C5D2C2E
title	The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes (en)
page(s)	wds:Q69041233-2436041F-9A51-4AED-9D9A-19E015DDA5FB
page(s)	4848-4855
instance of	wds:Q69041233-28958EEA-1EF1-4CF6-A5A0-0D0F8B00EFB1
instance of	scholarly article
main subject	wds:Q69041233-C67EF92C-CB28-482A-BB55-CB56A037ABAF
main subject	model membrane
PubMed ID	wds:Q69041233-4815D991-AFBD-4877-ABF9-18959008BA2C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2458757
PubMed ID	2458757
published in	wds:Q69041233-42D7142E-4471-408E-B338-9E00F9A3CAF3
published in	Biochemistry
issue	wds:Q69041233-89E445BD-9677-41F7-ACB6-7BBB5753A150
volume	wds:Q69041233-4C01A8F1-3709-44BA-B242-F6C610E999F6
issue	13
volume	27
number of pages	wds:Q69041233-A0476B0B-C18E-4903-BD77-C6E43F3A89DA
number of pages	8 (xsd:decimal)
DOI	wds:Q69041233-C62DF4E9-3A3B-4459-8C5B-27ACECD3A818
DOI	http://dx.doi.org/10.1021/BI00413A040
DOI	10.1021/BI00413A040
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69041233
is cites work of	The conducting form of gramicidin A is a right-handed double-stranded double helix Membrane Protein Crystallization in Lipidic Mesophases. Hosting Lipid Effects on the Crystallization and Structure of a Transmembrane Peptide Model ion channels: gramicidin and alamethicin Orientational constraints as three-dimensional structural constraints from chemical shift anisotropy: the polypeptide backbone of gramicidin A in a lipid bilayer Hydrophobic mismatch between proteins and lipids in membranes High-resolution mono- and multidimensional magic angle spinning 1H nuclear magnetic resonance of membrane peptides in nondeuterated lipid membranes and H2O. High-speed magic angle spinning solid-state 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers Novel gramicidin formulations in cationic lipid as broad-spectrum microbicidal agents The preference of tryptophan for membrane interfaces: insights from N-methylation of tryptophans in gramicidin channels Role of tryptophan residues in gramicidin channel organization and function The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A. Size-exclusion high-performance liquid chromatography in the study of the autoassociating antibiotic gramicidin A in micellar milieu. Monitoring gramicidin conformations in membranes: a fluorescence approach Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D Solid-state nuclear magnetic resonance characterization of gramicidin channel structure On the supramolecular organization of gramicidin channels. The elementary conducting unit is a dimer Protein stability and conformational rearrangements in lipid bilayers: linear gramicidin, a model system Gramicidin and gramicidin-lipid interactions Phase equilibria and molecular packing in the N,N-dimethyldodecylamine oxide/gramicidin D/water system studied by 2H nuclear magnetic resonance spectroscopy Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel Synthesis of acylated gramicidins and the influence of acylation on the interfacial properties and conformational behavior of gramicidin A Gramicidin single-channel properties show no solvent-history dependence Gramicidins A, B, and C form structurally equivalent ion channels. Polymorphic phospholipid phase transitions as tools to understand peptide-lipid interactions Interfacial properties of gramicidin and gramicidin-lipid mixtures measured with static and dynamic monolayer techniques A semi-empirical approach for the simulation of circular dichroism spectra of gramicidin A in a model membrane The effect of changes in gramicidin conformation on bilayer lipid properties Conformational trapping in a membrane environment: a regulatory mechanism for protein activity? HPLC study on the 'history' dependence of gramicidin A conformation in phospholipid model membranes High-resolution structure and dynamic implications for a double-helical gramicidin A conformer Modeling the membrane environment for membrane proteins The structure of an integral membrane peptide: a deuterium NMR study of gramicidin Decoupling of oxidative phosphorylation and photophosphorylation Gramicidin D conformation, dynamics and membrane ion transport Solvent history dependence of gramicidin-lipid interactions: a Raman and infrared spectroscopic study Role of phosphatidylethanolamine lipids in the stabilization of protein-lipid contacts The Influence of Lipid Bilayer Physicochemical Properties on Gramicidin A Conformer Preferences Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach Effect of structural transition of the host assembly on dynamics of an ion channel peptide: a fluorescence approach Monitoring membrane protein conformational heterogeneity by fluorescence lifetime distribution analysis using the maximum entropy method Design and characterization of gramicidin channels Polar groups in membrane channels: consequences of replacing alanines with serines in membrane-spanning gramicidin channels. Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry Deposition of highly resistive lipid bilayer on silicon–silicon dioxide electrode and incorporation of gramicidin studied by ac impedance spectroscopy Distinguishing gramicidin D conformers through two-dimensional infrared spectroscopy of vibrational excitons. Membrane structure and dynamics as viewed by solid-state NMR spectroscopy Effect of proteins on fluorophore lifetime heterogeneity in lipid bilayers The double pi pi 5.6 helix of gramicidin A predominates in unsaturated lipid membranes Design of peptide-membrane interactions to modulate single-file water transport through modified gramicidin channels Rational design, synthesis, and biological evaluation of lactam-bridged gramicidin A analogues: discovery of a low-hemolytic antibacterial peptide Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels. 13C solid-state NMR of gramicidin A in a lipid membrane Effect of Site-Specific Intermolecular Lysine-Tryptophan Interactions on the Aggregation of Gramicidin-Based Peptides Leading to Pore Formation in Lipid Membranes

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