Search results for "Protein secondary structure"

showing 10 items of 88 documents

Detecting Protein Aggregation on Cells Surface: Concanavalin A Oligomers Formation

2009

A number of neurodegenerative diseases involve protein aggregation and amyloid formation. Recently evidence has emerged indicating small-transient prefibrillar oligomers as the primary pathogenic agents. Noteworthy, strict analogies exist between the behaviour of cells in culture treated with misfolded non-pathogenic proteins and in pathologic conditions, this instance together with the observation that the oligomers and fibrils are characterised by common structural features suggest that common mechanisms for cytotoxicity could exists and have to be perused in common interactions involved in aggregation.We here report an experimental study on ConcanavalinA (ConA) aggregation and its effect…

0303 health sciencesbiologyAmyloidChemistryN&B confocal microscopy aggregates toxicityBiophysicsProtein aggregationCell membrane03 medical and health sciences0302 clinical medicinemedicine.anatomical_structureProtein structureBiochemistryConcanavalin ACell culturemedicinebiology.proteinBiophysicsMacromolecular crowdingProtein secondary structure030217 neurology & neurosurgery030304 developmental biologyBiophysical Journal
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FTIR spectroscopy studies of high pressure-induced changes in pork macromolecular structure

2019

Abstract High pressure processing (HPP) allows to extend the shelf life of meat and meat products by pressurization of microorganisms. At the same time, HPP can induce changes of the protein structure. Vacuum-packed pork chops were HPP-treated at 300, 600 MPa for 1 or 15 min. Samples of raw, cooked and HPP-treated meat muscles and juice were analysed to evaluate the structure of macromolecules. HPP caused visible discolouration of pork chops; hence, the colour of pork meat surface was tested. The lightness (colour component L*) was directly proportional to the applied pressure, probably due to the increased protein denaturation by high pressure. Pork meat muscle and juice samples were analy…

Absorption (pharmacology)ChemistryOrganic Chemistryfood and beveragesShelf lifeAnalytical ChemistryInorganic ChemistryPascalizationProtein structureAbsorption bandFood scienceFourier transform infrared spectroscopyProtein secondary structureSpectroscopyMacromoleculeJournal of Molecular Structure
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Interaction of theEscherichia colitransporter DctA with the sensor kinase DcuS: presence of functional DctA/DcuS sensor units

2012

The aerobic Escherichia coli C(4) -dicarboxylate transporter DctA and the anaerobic fumarate/succinate antiporter DcuB function as obligate co-sensors of the fumarate responsive sensor kinase DcuS under aerobic or anaerobic conditions respectively. Overproduction under anaerobic conditions allowed DctA to replace DcuB in co-sensing, indicating their functional equivalence in this capacity. In vivo interaction studies between DctA and DcuS using FRET or a bacterial two-hybrid system (BACTH) demonstrated their interaction. DctA-YFP bound to an affinity column and was able to retain DcuS. DctA shows substantial sequence and secondary structure conservation to Glt(Ph), the Na(+)/glutamate sympo…

AntiporterPlasma protein bindingBiologybiology.organism_classificationmedicine.disease_causeMicrobiologyPyrococcus horikoshiiTransmembrane domainBiochemistryHelixSymportermedicineMolecular BiologyEscherichia coliProtein secondary structureMolecular Microbiology
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1H-NMR studies on poly(oxyethylene)-bound oligopeptides

1983

Conformational studies on poly(oxyethylene)-bound homo-, oligo-, guest-host, and sequential peptides synthesized according to the liquid-phase method were carried out by means of 1H-nmr spectroscopy. The solubilizing effect of the C-terminal polymeric support allowed a thorough investigation of the secondary structure in solution.

BiomaterialsOligopeptideChemistryOrganic ChemistryBiophysicsProton NMROrganic chemistrymacromolecular substancesGeneral MedicineSpectroscopyBiochemistryProtein secondary structureBiopolymers
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Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1 1Edited by A. R. Fersht

1999

Negative factor (Nef) is a regulatory myristoylated protein of human immunodeficiency virus (HIV) that has a two-domain structure consisting of an anchor domain and a core domain separated by a specific cleavage site of the HIV proteases. For structural analysis, the HIV-1 Nef anchor domain (residues 2-57) was synthesized with a myristoylated and non-myristoylated N terminus. The structures of the two peptides were studied by1H NMR spectroscopy and a structural model was obtained by restrained molecular dynamic simulations. The non-myristoylated peptide does not have a unique, compactly folded structure but occurs in a relatively extended conformation. The only rather well-defined canonical…

ChemistryViral proteinStereochemistrySequence alignmentmedicine.disease_causeSerineCrystallographyProtein structureStructural BiologyHelixmedicinelipids (amino acids peptides and proteins)Molecular BiologyProtein secondary structurePeptide sequenceMyristoylationJournal of Molecular Biology
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Folding in vitro of light-harvesting chlorophyll a/b protein is coupled with pigment binding.

2002

The major light-harvesting chlorophyll a/b protein (LHCIIb) of the plant photosynthetic apparatus is able to self-organise in vitro. When the recombinant apoprotein, Lhcb1, is solubilised in the denaturing detergent sodium (or lithium) dodecylsulfate (SDS or LDS) and then mixed with chlorophylls and carotenoids under renaturing conditions, structurally authentic LHCIIb forms. Assembly of functional LHCIIb, as indicated by the establishment of energy transfer between complex-bound chlorophyll molecules, occurs in two apparent kinetic steps with time constants of 10 to 30 seconds and 50 to 300 seconds, depending on the reaction conditions. Here, we use circular dichroism (CD) in the far-UV ra…

Chlorophyll aCircular dichroismProtein FoldingCircular DichroismPigment bindingProtein domainPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesPhotochemistryPhotosynthesisProtein Structure SecondaryRecombinant Proteinschemistry.chemical_compoundPigmentchemistryStructural BiologyChlorophyllvisual_artvisual_art.visual_art_mediumMolecular BiologyProtein secondary structureMicellesSequence DeletionJournal of molecular biology
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Fluorescence and circular dichroism spectroscopy to understand the interactions between cyclodextrins and α-galactosidase from green coffee beans

2017

Abstract The potential of fluorescence measurement and circular dichroism spectroscopy (CDSP) to evaluate the interaction between cyclodextrins (CDs) (CD cavity size, concentration, pH, reaction time, and temperature as well as different side chain groups) and α-galactosidase was evaluated. A strong relationship was observed between α-galactosidase fluorescence intensity and CD cavity size, concentration, pH, reaction time, and temperature as well as different side chain groups. Therefore, it can be concluded that fluorescence intensity measurement can be a promising tool to ascertain β-CD-α-galactosidase interactions. CDSP is also an interesting tool to understand β-CD-α-galactosidase inte…

Circular dichroism010405 organic chemistryChemistryAnalytical chemistry010402 general chemistryPhotochemistry01 natural sciencesBiochemistryFluorescence0104 chemical sciencesFluorescence intensityα galactosidaseSide chainGreen coffeeProtein secondary structureInhibitory effectFood ScienceFood Bioscience
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Glucagon fibril polymorphism reflects differences in protofilament backbone structure

2010

Amyloid fibrils formed by the 29-residue peptide hormone glucagon at different concentrations have strikingly different morphologies when observed by transmission electron microscopy. Fibrils formed at low concentration (0.25 mg/mL) consist of two or more protofilaments with a regular twist, while fibrils at high concentration (8 mg/mL) consist of two straight protofilaments. Here, we explore the structural differences underlying glucagon polymorphism using proteolytic degradation, linear and circular dichroism, Fourier transform infrared spectroscopy (FTIR), and X-ray fiber diffraction. Morphological differences are perpetuated at all structural levels, indicating that the two fibril class…

Circular dichroismAmyloidProtein FoldingChemistryProtein StabilityCircular DichroismProteolytic enzymesmacromolecular substancesLinear dichroismFibrilGlucagonSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein Structure SecondaryCrystallographyX-Ray DiffractionStructural BiologySpectroscopy Fourier Transform InfraredSide chainFourier transform infrared spectroscopyProtein MultimerizationFiber diffractionMolecular BiologyProtein secondary structurePolymorphism Amyloid Glucagon Structural changesPeptide Hydrolases
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Inactivation and structural changes of polyphenol oxidase in quince ( Cydonia oblonga Miller) juice subjected to ultrasonic treatment

2020

Background Polyphenol oxidase (PPO) is considered a problem in the food industry because it starts browning reactions during fruit and vegetable processing. Ultrasonic treatment is a technology used to inactivate the enzyme; however, the mechanism behind PPO inactivation is still unclear. For this reason, the inactivation, aggregation, and structural changes in PPO from quince juice subjected to ultrasonic treatments were investigated. Different intensities and times of ultrasonic treatment were used. Changes in the activity, aggregation, conformation, and structure of PPO were investigated through different structural analyses. Results Compared to untreated juice, the PPO activity in treat…

Circular dichroismHot TemperatureChemical PhenomenaFood Handling030309 nutrition & dieteticsColorProtein aggregationPolyphenol oxidaseProtein Structure Secondary03 medical and health sciences0404 agricultural biotechnologyVegetablesBrowningUltrasonicsParticle SizeRosaceaeProtein secondary structurePlant Proteinschemistry.chemical_classification0303 health sciencesNutrition and Dieteticsbusiness.industryChemistryCircular DichroismUltrasound04 agricultural and veterinary sciencesHydrogen-Ion Concentration040401 food scienceProtein tertiary structureMaillard ReactionFruit and Vegetable JuicesEnzymeFruitBiophysicsbusinessAgronomy and Crop ScienceCatechol OxidaseFood ScienceBiotechnologyJournal of the Science of Food and Agriculture
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Isolation and characterization of haemoporin, an abundant haemolymph protein from Aplysia californica.

2003

In the present study, we show the isolation and characterization of the protein haemoporin, which constitutes the second most abundant protein fraction in the haemolymph of the marine gastropod Aplysia californica. Although Aplysia is commonly used to investigate the molecular basis of learning, not much is known about the proteins in its haemolymph, which is in contact with the neurons owing to the open circulatory system of molluscs. In the native state, haemoporin is a macromolecular complex forming a cylinder with a central solvent-filled pore. The native complex most probably is a homopentamer made up from 70 kDa subunits with a molecular mass of 360 kDa and a sedimentation coefficient…

Circular dichroismanimal structuresMolecular Sequence DataMegathura crenulataBiochemistrySequence Analysis ProteinHemolymphHemolymphAplysiaNative stateAnimalsAmino Acid SequenceMolecular BiologyProtein secondary structurebiologyMolecular massCircular DichroismCell BiologyAnatomyBlood Proteinsbiology.organism_classificationMolecular WeightMicroscopy ElectronSpectrometry FluorescenceBiochemistryAplysiaProtein quaternary structureElectrophoresis Polyacrylamide GelUltracentrifugationResearch ArticleThe Biochemical journal
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