Search results for "Conformational stability"

showing 3 items of 3 documents

Structural Tuning and Conformational Stability of Aromatic Oligoamide Foldamers

2017

A series of aromatic oligoamide foldamers with two or three pyridine-2,6-dicarboxamide units as their main folding motifs and varying aromatic building blocks as linkers have been synthetized to study the effects of the structural variation on the folding properties and conformational stability. Crystallographic studies showed that in the solid state the central linker unit either elongates the helices and more open S-shaped conformations, compresses the helices to more compact conformations or acts as a rigid spacer separating the pyridine-2,6-dicarboxamide units, which for their part add the predictability of the conformational properties. Multidimensional NMR studies showed that, even in…

010405 organic chemistryChemistryHydrogen bondOrganic ChemistrySolid-stateGeneral ChemistryNuclear magnetic resonance spectroscopy010402 general chemistry01 natural sciencesstructuresCatalysis0104 chemical sciencesFolding (chemistry)Crystallographyaromatic oligoamide foldamersConformational stabilityLinkerta116Chemistry: A European Journal
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Enhanced β-turn conformational stability of tripeptides containing Δphe in cis over trans configuration

2013

Conformations of three pairs of dehydropeptides with the opposite configuration of the Delta Phe residue, Boc-Gly-Delta(Z/E)Phe-Phe-p-NA (Z- p -NA and E- p -NA), Boc-Gly-Delta(Z/E)Phe-Phe-OMe (Z-OMe and E-OMe), and Boc-Gly-Delta(Z/E)Phe-Phe-OH (Z-OH and E-OH) were compared on the basis of CD and NMR studies in MeOH, TFE, and DMSO. The CD results were used as the additional input data for the NMR-based calculations of the detailed solution conformations of the peptides. It was found that Z- p -NA, E- p -NA, Z-OMe, and Z-OH adopt the beta-turn conformations and E-OMe and E-OH are unordered. There are two overlapping type III beta-turns in Z- p -NA, type II' beta-turn in E- p -NA, and type II …

Dehydropeptide conformationCircular dichroismMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineClinical BiochemistryTripeptideCircular dichroismTemperature coefficients of amide protonsBiochemistryNuclear magnetic resonancechemistry.chemical_compoundResidue (chemistry)Trans configurationchemistry [Oligopeptides]Amideotorhinolaryngologic diseasesHydrogen bondProtein StabilityDehydropeptidesCircular DichroismOrganic ChemistryStereoisomerismchemistryIntramolecular forceddc:540Dehydrophenylalanine configurationchemical synthesis [Oligopeptides]Conformational stabilitychemistry [Phenylalanine]OligopeptidesAmino Acids
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Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin

2004

Hemocyanin sequences allineament shows the presence of highly invariant regions especially in the active site and in the tight intersubunits interaction sites. Comparing the aminoacids in contact regions between monomers is possible to interpret the stability of hexamers.

Protein Conformationmedicine.medical_treatmentGeneral Physics and AstronomyBiologyPenaeus monodon03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePenaeidaeStructural BiologymedicineAnimalsGeneral Materials Science030304 developmental biology0303 health sciencesEcologyActive siteHemocyaninCell Biologybiology.organism_classificationOxygenMonomerchemistryHemocyaninsBiophysicsbiology.proteinProtein quaternary structureConformational stability030217 neurology & neurosurgeryOxygen binding
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