Search results for "folding"

showing 10 items of 330 documents

Evaluation of Fused Pyrrolothiazole Systems as Correctors of Mutant CFTR Protein.

2021

Cystic fibrosis (CF) is a genetic disease caused by mutations that impair the function of the CFTR chloride channel. The most frequent mutation, F508del, causes misfolding and premature degradation of CFTR protein. This defect can be overcome with pharmacological agents named “correctors”. So far, at least three different classes of correctors have been identified based on the additive/synergistic effects that are obtained when compounds of different classes are combined together. The development of class 2 correctors has lagged behind that of compounds belonging to the other classes. It was shown that the efficacy of the prototypical class 2 corrector, the bithiazole corr-4a, could be impr…

Yellow fluorescent proteinProtein FoldingCystic FibrosisMutantPharmaceutical ScienceCystic Fibrosis Transmembrane Conductance RegulatorCarboxamidemedicine.disease_cause01 natural sciencesAnalytical Chemistrychemistry.chemical_compoundMutant ProteinDrug DiscoveryMoietyCFTR potentiatorCFTRchemistry.chemical_classification0303 health sciencesMutationbiologyChemistryChemistry (miscellaneous)Chloride channelMolecular MedicineHumanStereochemistrymedicine.drug_classCFTR correctorArticleF508del-CFTRlcsh:QD241-44103 medical and health scienceslcsh:Organic chemistrymedicineHumansBenzodioxolesPhysical and Theoretical ChemistryThiazoleCystic Fibrosi030304 developmental biology010405 organic chemistryOrganic ChemistryAminoimidazole Carboxamide0104 chemical sciencesThiazolesMutationbiology.proteinMutant ProteinsBenzodioxoleTricyclicMolecules (Basel, Switzerland)
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Unfolding of saddle-nodes and their Dulac time

2016

Altres ajuts: UNAB10-4E-378, co-funded by ERDF "A way to build Europe" and by the French ANR-11-BS01-0009 STAAVF. In this paper we study unfoldings of saddle-nodes and their Dulac time. By unfolding a saddle-node, saddles and nodes appear. In the first result (Theorem A) we give a uniform asymptotic expansion of the trajectories arriving at the node. Uniformity is with respect to all parameters including the unfolding parameter bringing the node to a saddle-node and a parameter belonging to a space of functions. In the second part, we apply this first result for proving a regularity result (Theorem B) on the Dulac time (time of Dulac map) of an unfolding of a saddle-node. This result is a b…

[ MATH.MATH-DS ] Mathematics [math]/Dynamical Systems [math.DS][MATH.MATH-DS]Mathematics [math]/Dynamical Systems [math.DS]Block (permutation group theory)Dynamical Systems (math.DS)Space (mathematics)01 natural sciencesCombinatoricsQuadratic equationFOS: MathematicsMathematics - Dynamical Systems0101 mathematicsBifurcationSaddleMathematicsPeriod functionApplied MathematicsUnfolding of a saddle-node010102 general mathematics16. Peace & justice010101 applied mathematicsMSC: 34C07Asymptotic expansions34C07Node (circuits)Asymptotic expansionAnalysis
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One-parameter family of Clairaut-Liouville metrics

2007

Riemannian metrics with singularities are considered on the $2$-sphere of revolution. The analysis of such singularities is motivated by examples stemming from mechanics and related to projections of higher dimensional (regular) sub-Riemannian distributions. An unfolding of the metrics in the form of an homotopy from the canonical metric on $\SS^2$ is defined which allows to analyze the singular case as a limit of standard Riemannian ones. A bifurcation of the conjugate locus for points on the singularity is finally exhibited.

[ MATH.MATH-OC ] Mathematics [math]/Optimization and Control [math.OC]space mechanics49K15 53C20 70Q05$2$-sphere of revolution[MATH.MATH-OC] Mathematics [math]/Optimization and Control [math.OC][MATH.MATH-OC]Mathematics [math]/Optimization and Control [math.OC]Mathematics::Differential Geometryunfolding
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Hsp60, a Novel Target for Antitumor Therapy: Structure-Function Features and Prospective Drugs Design

2013

Heat shock protein 60 kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60's function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these …

animal structuresBinding pocketCellAntineoplastic Agentschemical and pharmacologic phenomenaComputational biologyBiologyBioinformaticsFunctional domaincomplex mixturesChaperoninStructure-Activity RelationshipNeoplasmsHeat shock proteinDrug DiscoverymedicineHumansPharmacologyCompound dockingSettore BIO/16 - Anatomia UmanaCell growthfungiSettore CHIM/06 - Chimica OrganicaChaperonin 60Hsp60Settore CHIM/08 - Chimica FarmaceuticaCytoprotectionGroELmedicine.anatomical_structureSettore CHIM/03 - Chimica Generale E InorganicaCancer treatmentDrug DesignChaperone (protein)biology.proteinHSP60Protein foldingEpolactaeneCurrent Pharmaceutical Design
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Hsp60 in Modifications of Nervous System Homeostasis and Neurodegeneration

2019

Hsp60 is a critical chaperonin for its role in preserving cell survival and protecting mitochondria against stress conditions. Indeed, mutations or malfunctions of Hsp60 are involved in several human diseases, either genetic or acquired, some of them affecting also the brain. In this chapter, we present several experimental observations supporting the role of Hsp60 in some neurodegenerative diseases. Further, Hsp60, as multifunctional protein, contributes to the protein folding system, to protect mitochondria and is involved in several other cellular pathways that are known to be affected in these diseases. Furthermore, due to its role outside of the mitochondria and in the extracellular fl…

animal structuresfungiNeurodegenerationchemical and pharmacologic phenomenamacromolecular substancesBiologyMitochondrionmedicine.diseasecomplex mixturesMicrovesiclesCell biologyChaperoninmedicineHSP60Protein foldingNeuroinflammationHomeostasis
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High Resolution Solution NMR Structure of the Z Domain of Staphylococcal Protein A. Analysis of Secondary Structure for Free Z Domain and Bounded to …

1997

Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylcoccus aureus. It exhibits tight binding to many IgG, IgA and IgM molecules at site(s) different from antigen-combining site. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are important targets for protein engineering efforts and for the development of computational approaches for de novo protein folding.

biology'de novo' protein foldingChemistryStaphylococcal proteinProtein engineeringbiology.organism_classificationCrystallographyBiochemistryDomain (ring theory)biology.proteinAntibodyProtein AProtein secondary structureBacteria
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Local vs global motions in protein folding

2013

It is of interest to know whether local fluctuations in a polypeptide chain play any role in the mechanism by which the chain folds to the native structure of a protein. This question is addressed by analyzing folding and non-folding trajectories of a protein; as an example, the analysis is applied to the 37-residue triple β-strand WW domain from the Formin binding protein 28 (FBP28) (PDB ID: 1E0L). Molecular dynamics (MD) trajectories were generated with the coarse-grained united-residue force field, and one- and two-dimensional free-energy landscapes (FELs) along the backbone virtual-bond angle θ and backbone virtual-bond-dihedral angle γ of each residue, and principal components, respect…

biologyChemistryBinding proteinProtein Data Bank (RCSB PDB)NanotechnologyForce field (chemistry)ArticleComputer Science ApplicationsWW domainMolecular dynamicsForminsPrincipal component analysisbiology.proteinProtein foldingPhysical and Theoretical ChemistryBiological system
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Redox Biochemistry of the Genetic Code.

2021

New findings on the chemistry of the amino acids, their role in protein folding, and their sequential primordial introduction have uncovered concealed causalities in genetic code evolution. The genetically encoded amino acids successively provided (i) membrane anchors, (ii) halophilic protein folds, (iii) mesophilic protein folds, (iv) metal ligation, and (v) antioxidation.

chemistry.chemical_classification0303 health sciencesModels GeneticChemistryProteinsGenetic codeBiochemistryRedoxHalophileEnzyme catalysisAmino acidEvolution Molecular03 medical and health sciences0302 clinical medicineBiochemistryAbiogenesisGenetic CodeProtein foldingAmino AcidsMolecular BiologyOxidation-Reduction030217 neurology & neurosurgery030304 developmental biologyTrends in biochemical sciences
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Helix–Coil Transition in Cylindrical Brush Polymers with Poly-l-lysine Side Chains

2012

Cylindrical brush polymers with poly-l-lysine side chains were prepared by grafting lysine NCA from a macroinitiator via living ring-opening polymerization. The main chain degree of polymerization of the methacrylate main chain was Pw = 870, the side chains consisted of 25 and 55 lysine repeat units, respectively. Upon deprotection, the cylindrical brush polymers in 0.005 M NaBr exhibited an almost rodlike conformation with a Kuhn statistical segment length of several hundred nanometers. Cryo-TEM as well as AFM in aqueous solution clearly demonstrated pronounced undulations along the main chain at low ionic strength which could not be detected at higher salt concentrations. With increasing …

chemistry.chemical_classificationAqueous solutionMaterials sciencePolymers and PlasticsOrganic ChemistryPolymerDegree of polymerizationMethacrylateInorganic ChemistryFolding (chemistry)CrystallographyPolymerizationchemistryHelixMaterials ChemistrySide chainMacromolecules
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Epoxide Hydrolases: Structure, Function, Mechanism, and Assay

2005

Epoxide hydrolases are a class of enzymes important in the detoxification of genotoxic compounds, as well as in the control of physiological signaling molecules. This chapter gives an overview on the function, structure, and enzymatic mechanism of structurally characterized epoxide hydrolases and describes selected assays for the quantification of epoxide hydrolase activity.

chemistry.chemical_classificationCell signaling1303 BiochemistryStereochemistry10050 Institute of Pharmacology and Toxicology610 Medicine & healthEpoxide hydrolase activityEnzymeBiochemistrychemistryDetoxificationEpoxide Hydrolases1312 Molecular Biology570 Life sciences; biologyProtein foldingEpoxide hydrolaseFunction (biology)
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