Search results for "Gramicidin A"

showing 3 items of 3 documents

HPLC study on the ‘history’ dependence of gramicidin A conformation in phospholipid model membranes

1989

AbstractA novel HPLC methodology for the study of gramicidin A reconstituted in model membranes has been tested in comparison with circular dichroism data. It is shown that this chromatographic technique not only corroborates most of the recent spectroscopic results but allows one to explain them in terms of mass fractions of different actual conformational species of GA in the phospholipid assemblies. In particular, the dependence of the inserted peptide configuration on the organic solvent and other parameters involved in the ‘history’ of the sample preparation and handling has been analyzed by HPLC in two phospholipid model systems: small unilamellar vesicles and micelles. Moreover, a sl…

Circular dichroismProtein ConformationMolecular ConformationBiophysicsPhospholipidPeptideBiochemistryHigh-performance liquid chromatographyMicellechemistry.chemical_compoundStructural BiologyGramicidin A conformationGeneticsGramicidin ASample preparationMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChromatographyChemistryCircular DichroismGramicidinMembranes ArtificialCell BiologyModels TheoreticalCDMembraneLiposomesPhospholipid vesiclePhosphatidylcholinesHPLCFEBS Letters
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HPLC demonstration that an all Trp--Phe replacement in gramicidin A results in a conformational rearrangement from beta-helical monomer to double-str…

1995

We have taken advantage of our previously reported high performance liquid chromatographic (HPLC) strategy to investigate the conformational behavior of the optically reversed gramicidin M (gM-), an analog of gramicidin A with all tryptophans replaced by phenylalanines, in different model membranes. It is quantitatively demonstrated for the first time that once inserted in the lipid environment, gM- (unlike the native peptide) undergoes a conformational transition from beta-helical monomers to thermodynamically stable double-stranded dimers. This transition is faster the higher the incubation temperature and can be neatly observed in both small unilamellar phospholipid vesicles and lysophos…

Protein ConformationDimerPhenylalanineBiophysicsPeptideBiochemistryMicelleHigh-performance liquid chromatographyIon ChannelsProtein Structure Secondarychemistry.chemical_compoundStructure-Activity RelationshipGramicidin AOrganic chemistryMolecular BiologyChromatography High Pressure Liquidchemistry.chemical_classificationChemistrytechnology industry and agricultureGramicidinTryptophanMembrane ProteinsMembranes ArtificialCell BiologyCrystallographyMembraneMonomerlipids (amino acids peptides and proteins)Double strandedBiochemical and biophysical research communications
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Time-dependent monomerization of gramicidin A, enhanced by phosphatidylcholine in non-polar solvents

1986

Abstract The usefulness of size-exclusion high-performance liquid chromatography for the study of gramicidin A dimer—monomer conformational equilibrium in non

chemistry.chemical_compoundChromatographyChemistryPhosphatidylcholineOrganic Chemistrytechnology industry and agriculturepolycyclic compoundsGramicidin Alipids (amino acids peptides and proteins)Non polarGeneral MedicineBiochemistryAnalytical ChemistryJournal of Chromatography A
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