Search results for "Structural motif"

showing 10 items of 13 documents

Density functional study of Cu2+-phenylalanine complex under micro-solvation environment

2013

Abstract We present an atomistic study carried out using density functional calculations including structural relaxations and Car–Parrinello Molecular Dynamics (CPMD) simulations, aiming to investigate the structures of phenylalanine-copper (II) ([Phe-Cu] 2+ ) complexes and their micro-solvation processes. The structures of the [Phe-Cu] 2+ complex with up to four water molecules are optimized using the B3LYP/6-311++G** model in gas phase to identify the lowest energy structures at each degree of solvation ( n  = 0–4). It is found that the phenylalanine appears to be in the neutral form in isolated and mono-hydrated complexes, but in the zwitterionic form in other hydrated complexes (with n …

Models MolecularCar–Parrinello molecular dynamicsPhenylalanineMolecular ConformationDFTMolecular dynamicsMaterials ChemistryMicro-solvationMoleculePhysical and Theoretical ChemistryPhenylalanine-copper (II) complexStructural motifta116Spectroscopyta114LigandHydrogen bondChemistrySolvationHydrogen BondingComputer Graphics and Computer-Aided DesignCrystallographySolvation shellModels ChemicalCPMDCopperJOURNAL OF MOLECULAR GRAPHICS AND MODELLING
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A New Structural Motif for an Enantiomerically Pure Metallosupramolecular Pd4L8Aggregate by Anion Templating

2014

An enantiomerically pure BINOL-based bis(3-pyridyl) ligand 1 assembles into a homochiral [Pd4(1)8] complex upon coordination to tetravalent PdII ions. The formation of this aggregate is templated by two tetrafluoroborate counterions that are encapsulated in two peripheral cavities. The resulting structure is a new structural motif for this kind of metallosupramolecular assemblies that arranges the palladium ions in a distorted tetrahedral fashion and forces ligand 1 to adopt two different conformations. Both phenomena are unique and cause an overall three-dimensional structure that has another confined, chiral, and hydrophilic central cavity.

chemistry.chemical_classificationTetrafluoroborateLigandStereochemistryAggregate (data warehouse)chemistry.chemical_elementGeneral ChemistryCatalysisIonCrystallographychemistry.chemical_compoundchemistrySelf-assemblyCounterionStructural motifta116PalladiumAngewandte Chemie International Edition
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Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

2018

15 páginas, 6 figuras, 1 tabla.

0301 basic medicineGoodpasture’s diseaseAddenda and ErrataRandom hexamerBiochemistryEpitopelaw.invention03 medical and health sciencesAlport's syndrome0302 clinical medicineGoodpasture's diseaselawMissense mutationGeneral Materials ScienceAlport’s syndromeStructural motifNetwork assemblyCrystallographyGoodpasture's diseaseChemistry(IV)NC1 hexamersStructural proteinCollagen type IVGeneral ChemistryCondensed Matter PhysicsResearch PapersFolding (chemistry)030104 developmental biologyQD901-999BiophysicsRecombinant DNA030217 neurology & neurosurgeryAlport syndrome
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A Stevedore's protein knot.

2009

Protein knots, mostly regarded as intriguing oddities, are gradually being recognized as significant structural motifs. Seven distinctly knotted folds have already been identified. It is by and large unclear how these exceptional structures actually fold, and only recently, experiments and simulations have begun to shed some light on this issue. In checking the new protein structures submitted to the Protein Data Bank, we encountered the most complex and the smallest knots to date: A recently uncovered α-haloacid dehalogenase structure contains a knot with six crossings, a so-called Stevedore knot, in a projection onto a plane. The smallest protein knot is present in an as yet unclassified …

Protein FoldingHydrolasesProtein ConformationComputational Biology/Macromolecular Structure Analysis02 engineering and technologyBiologyMolecular Dynamics SimulationComputational Biology/Molecular DynamicsCombinatorics03 medical and health sciencesCellular and Molecular NeuroscienceKnot (unit)Protein structureGeneticsStructural motifDatabases ProteinMolecular Biologylcsh:QH301-705.5Ecology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesTopological complexityQuantitative Biology::BiomoleculesEcologycomputer.file_format021001 nanoscience & nanotechnologyProtein Data BankMathematics::Geometric TopologyComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Modeling and SimulationProtein foldingStevedore knot0210 nano-technologySingle loopcomputerResearch ArticlePLoS Computational Biology
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SHAPE MATTERS: EFFECT OF POINT MUTATIONS ON RNA SECONDARY STRUCTURE

2013

A suitable model to dive into the properties of genotype-phenotype landscapes is the relationship between RNA sequences and their corresponding minimum free energy secondary structures. Relevant issues related to molecular evolvability and robustness to mutations have been studied in this framework. Here, we analyze the one-mutant neighborhood of the predicted secondary structure of 46 different RNAs, including tRNAs, viroids, larger molecules such as Hepatitis-δ virus, and several random sequences. The probability distribution of the effect of point mutations in linear structural motifs of the secondary structure is well fit by Pareto or Lognormal probability distributions functions, indep…

0106 biological sciencesGenetics0303 health sciencesPoint mutationRNARobustness (evolution)Computational biologyBiology010603 evolutionary biology01 natural sciencesNucleic acid secondary structureEvolvability03 medical and health sciencesControl and Systems EngineeringProbability distributionStructural motifRNA secondary structure sequence-structure map mutational effects linear motifsProtein secondary structure030304 developmental biologyAdvances in Complex Systems
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Mo-Based Oxidizers as Powerful Tools for the Synthesis of Thia- and Selenaheterocycles.

2019

A highly efficient synthetic protocol for the synthesis of thia- and selenaheterocycles has been developed. By employing a MoCl5 -mediated intramolecular dehydrogenative coupling reaction, a broad variety of structural motifs was isolated in yields up to 94 %. The electrophilic key transformation is tolerated by several labile moieties like halides and tertiary alkyl groups. Due to the use of disulfide or diselenide precursors, a high atom efficiency was achieved.

chemistry.chemical_classificationcyclization010405 organic chemistryChemistryoxidationOrganic ChemistryHalideGeneral Chemistry010402 general chemistry01 natural sciencesCombinatorial chemistryCatalysisCoupling reactionC−H activationsulfur heterocycles0104 chemical sciencesDiselenidemolybdenumAtom economyIntramolecular forceElectrophileStructural motifAlkylChemistry (Weinheim an der Bergstrasse, Germany)
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Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues

2021

Abstract Post-translational modified thiazole–amino acid (Xaa–Tzl) residues have been found in macrocyclic peptides (e.g., thiopeptides and cyanobactins), which mostly inhibit protein synthesis in Gram + bacteria. Conformational study of the series of model compounds containing this structural motif with alanine, dehydroalanine, dehydrobutyrine and dehydrophenylalanine were performed using DFT method in various environments. The solid-state crystal structure conformations of thiazole–amino acid residues retrieved from the Cambridge Structural Database were also analysed. The studied structural units tend to adopt the unique semi-extended β2 conformation; which is stabilised mainly by N–H⋯N…

0301 basic medicineStereochemistryClinical BiochemistryNon-standard amino acidsMolecular ConformationRamachandran map010402 general chemistryRing (chemistry)01 natural sciencesBiochemistryDFT03 medical and health scienceschemistry.chemical_compoundDehydroalanineAmino AcidsStructural motifThiazoleOxazoleAlaninechemistry.chemical_classificationHydrogen bondNon-standard amino AIDSHydrogen bondOrganic ChemistryHydrogen Bonding0104 chemical sciencesAmino acidThiazoles030104 developmental biologyConformational analysischemistryOriginal ArticleThiazolePeptidesAmino Acids
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Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

2013

alpha-Helical hairpins, consisting of a pair of closely spaced transmembrane (TM) helices that are connected by a short interfacial turn, are the simplest structural motifs found in multi-spanning membrane proteins. In naturally occurring hairpins, the presence of polar residues is common and predicted to complicate membrane insertion. We postulate that the pre-packing process offsets any energetic cost of allocating polar and charged residues within the hydrophobic environment of biological membranes. Consistent with this idea, we provide here experimental evidence demonstrating that helical hairpin insertion into biological membranes can be driven by electrostatic interactions between clo…

Models MolecularBioquímicaProtein FoldingGlycosylationMolecular Sequence Datamembrane integrationEndoplasmic Reticulumsalt bridgeProtein Structure SecondaryTurn (biochemistry)Viral Proteins03 medical and health sciencesProtein structureStructural BiologyComputer SimulationAmino Acid SequenceAmino AcidsStructural motifMolecular Biologytranslocon030304 developmental biology0303 health sciencesBinding SitesChemistry030302 biochemistry & molecular biologyProteïnes de membranaBiochemistry and Molecular BiologyMembrane ProteinsBiological membraneTransloconelectrostatic interactionsTransmembrane proteinProtein Structure TertiaryPoliovirusProtein TransportCrystallographyTransmembrane domainhelical hairpinMembrane proteinMutationBiophysicsElectrophoresis Polyacrylamide GelHydrophobic and Hydrophilic InteractionsBiokemi och molekylärbiologi
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A novel RNA-binding motif in influenza A virus non-structural protein 1.

1997

The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2′ forms a novel arginine-rich nucleic acid binding motif.

Helix bundleModels MolecularBinding SitesMagnetic Resonance SpectroscopyChemistryStructural proteinViral Nonstructural ProteinsAntiparallel (biochemistry)medicine.disease_causeVirusProtein Structure SecondaryBiochemistryStructural BiologyInfluenza A virusInfluenza A virusmedicineNucleic acidRNAStructural motifMolecular BiologySterile alpha motifDimerizationNature structural biology
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Molecular characterisation, evolution and expression analysis of g-type lysozymes in Ciona intestinalis

2017

Lysozyme is an important defense molecule of the innate immune system. Known for its bactericidal properties, lysozyme catalyzes the hydrolysis of b-(1,4)-glycosidic bonds between the N-acetyl glucosamine and N-acetyl muramic acid in the peptidoglycan layer of bacterial cell walls. In this study, the complete coding sequence of four g-type lysozymes were identified in Ciona intestinalis. Phylogenetic analysis and modelling supported the hypothesis of a close relationship with the vertebrate g-type lysozymes suggesting that the C. intestinalis g-type lysozyme genes (CiLys-g1, Cilys-g2, CiLys-g3, CiLys-g4) share a common ancestor in the chordate lineage. Protein motif searches indicated that …

0301 basic medicineLipopolysaccharidesImmunologySettore BIO/05 - ZoologiaChordateBacterial cell structureMicrobiologyEvolution Molecular03 medical and health scienceschemistry.chemical_compound0302 clinical medicineBacteriolysisGeeseAnimalsCiona intestinalisCloning MolecularStructural motifGeneCells CulturedPhylogenyInnate immune systembiologyBacterial Infectionsbiology.organism_classificationBiological EvolutionImmunity InnateCiona intestinalisAscidian Lysozymes g-type Inflammation LPS Ciona intestinalis030104 developmental biologyBiochemistrychemistry030220 oncology & carcinogenesisPharynxMuramidasePeptidoglycanLysozymeTranscriptomeDevelopmental Biology
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