Search results for "folding"

showing 10 items of 330 documents

Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously.

2008

This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (alpha-helix and beta-hairpin) and independent secondary-structure elements. The design was based on the use of conformationally restricted peptide libraries. Structural characterization by NMR revealed that the peptides were stable and did not show any long-range NOE interactions between the N-terminal beta-hairpin and the C-terminal alpha-helix. These results suggest that the two elements of secondary structure are stable and well folded. Copyright (C) 2008 European Peptide Society and John Wiley & Sons. Ltd.

Models MolecularProtein FoldingStereochemistryMolecular Sequence DataPeptideBiochemistryBivalent (genetics)Protein Structure Secondarybivalent peptidesNMR spectroscopyStructural BiologyDrug DiscoveryAmino Acid SequenceMolecular BiologyProtein secondary structureNuclear Magnetic Resonance BiomolecularPharmacologychemistry.chemical_classificationconformationally definedChemistrypeptide librariesOrganic ChemistryGeneral MedicineNuclear magnetic resonance spectroscopyCombinatorial chemistryProtein Structure Tertiarypeptide designMolecular MedicinePeptidesJournal of peptide science : an official publication of the European Peptide Society
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Multiscale simulations of protein landscapes: Using coarse-grained models as reference potentials to full explicit models

2010

Evaluating the free-energy landscape of proteins and the corresponding functional aspects presents a major challenge for computer simulation approaches. This challenge is due to the complexity of the landscape and the enormous computer time needed for converging simulations. The use of simplified coarse-grained (CG) folding models offers an effective way of sampling the landscape but such a treatment, however, may not give the correct description of the effect of the actual protein residues. A general way around this problem that has been put forward in our early work (Fan et al., Theor Chem Acc 1999;103:77-80) uses the CG model as a reference potential for free-energy calculations of diffe…

Models MolecularProtein FoldingWork (thermodynamics)Protein ConformationChemistryMolecular Sequence DataStatic ElectricityProteinsSampling (statistics)Hydrogen BondingFolding (DSP implementation)Ph changesBiochemistryArticleStructure function correlationStructural BiologyKey (cryptography)Computer SimulationProtein foldingAmino Acid SequenceMolecular BiologyAlgorithmMathematicsSimulationEnergy (signal processing)Proteins: Structure, Function, and Bioinformatics
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The regulation mechanism for the auto-inhibition of binding of human filamin A to integrin.

2009

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Human filamins are large actin cross-linking proteins that connect integrins to the cytoskeleton. Filamin binding to the cytoplasmic tail of beta integrins has been shown to prevent integrin activation in cells, which is important for controlling cell adhesion and migration. The molecular-level mechanism for filamin binding to integrin has been unclear, however, as it was recently demonstrated that filamin undergoes intramolecular auto-inhibition of integrin binding. In this study, using steered molecular dynamics simulations, we f…

Models MolecularProtein Foldinganimal structuresIntegrin beta ChainsFilaminsmacromolecular substancesBiologyFilaminCD49cCollagen receptorFilamin bindingPhosphoserineContractile ProteinsStructural BiologyHumansPhosphorylationMolecular BiologyIntegrin bindingBinding SitesMicrofilament ProteinsActin cytoskeletonCell biologybody regionsIntegrin alpha Mbiology.proteinIntegrin beta 6Stress MechanicalPeptidesProtein BindingJournal of molecular biology
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When two turn into one: evolution of membrane transporters from half modules

2014

Abstract The recently increasing number of atomic structures for active transporters has not only revealed strong conservation in the architecture of sequence-unrelated transporter families, but also identified a unifying element called the ‘inverted repeat topology,’ which is found in nearly all transporter folds to date. Indeed, most membrane transporters consist of two or more domains with similar structure, so-called repeats. It is tempting to speculate that transporters have evolved by duplication of one repeat followed by gene fusion and modification events. An intriguing question is, whether recent genes encoding such a ‘half-transporter’ still exist as independent folding units. Alt…

Models MolecularProtein FoldingbiologyProtein familyProtein ConformationMembrane transport proteinInverted repeatClinical BiochemistryMembrane Transport ProteinsTransporterBiochemistryEvolution MolecularProtein structureBiochemistryEvolutionary biologyGene duplicationbiology.proteinAnimalsHumansProtein foldingMolecular BiologyGeneBiological Chemistry
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Folding and stability of the aquaglyceroporin GlpF: Implications for human aqua(glycero)porin diseases

2015

AbstractAquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure ca…

Models MolecularProtein activityAmino Acid MotifsMolecular Sequence DataBiophysicsGene ExpressionPorinsAquaporinDiabetes Insipidus NephrogenicEndoplasmic-reticulum-associated protein degradationAquaporinsBiochemistryCataractProtein Structure SecondaryProtein structureNeoplasmsEscherichia coliGlpFHumansProtein foldingConserved SequenceProtein StabilityChemistryurogenital systemEscherichia coli ProteinsAquaporinWaterCell BiologyTransmembrane proteinCell biologyFolding (chemistry)Membrane proteinBiochemistryMembrane proteinPorinProtein foldingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Single-Molecule FRET Reveals a Cooperative Effect of Two Methyl Group Modifications in the Folding of Human Mitochondrial tRNALys

2011

Summary Using a combination of advanced RNA synthesis techniques and single molecule spectroscopy, the deconvolution of individual contributions of posttranscriptional modifications to the overall folding and stabilization of human mitochondrial tRNA Lys is described. An unexpected destabilizing effect of two pseudouridines on the native tRNA folding was evidenced. Furthermore, the presence of m 2 G10 alone does not facilitate the folding of tRNA Lys , but a stabilization of the biologically functional cloverleaf shape in conjunction with the principal stabilizing component m 1 A9 exceeds the contribution of m 1 A alone. This constitutes an unprecedented cooperative effect of two nucleotide…

Models MolecularRNA StabilityMolecular Sequence DataClinical BiochemistryContext (language use)BiologyBiochemistryOrganophosphorus CompoundsDrug DiscoveryFluorescence Resonance Energy TransferHumansNucleotideMagnesiumTRNA foldingColoring AgentsMolecular Biologychemistry.chemical_classificationPharmacologyBase SequenceOligonucleotideRNAGeneral MedicineSingle-molecule FRETMitochondriaFolding (chemistry)chemistryBiochemistryTransfer RNABiophysicsNucleic Acid ConformationRNA Transfer LysMolecular MedicinePseudouridineChemistry & Biology
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cDNA Cloning and Functional Expression of Jerdostatin, a Novel RTS-disintegrin from Trimeresurus jerdonii and a Specific Antagonist of the α1β1 Integ…

2005

Jerdostatin represents a novel RTS-containing short disintegrin cloned by reverse transcriptase-PCR from the venom gland mRNA of the Chinese Jerdons pit viper Trimeresurus jerdonii. The jerdostatins precursor cDNA contained a 333-bp open reading frame encoding a signal peptide, a pre-peptide, and a 43-amino acid disintegrin domain, whose amino acid sequence displayed 80% identity with that of the KTS-disintegrins obtustatin and viperistatin. The jerdostatin cDNA structure represents the first complete open reading frame of a short disintegrin and points to the emergence of jerdostatin from a short-coding gene. The different residues between jerdostatin and obtustatin/viperistatin are segreg…

Models MolecularSignal peptideProtein FoldingDNA ComplementaryMagnetic Resonance SpectroscopyProtein ConformationDisintegrinsMolecular Sequence DataIntegrinMutantGene ExpressionPeptide MappingBiochemistryIntegrin alpha1beta1Open Reading FramesExocrine GlandsComplementary DNACrotalid VenomsDisintegrinAnimalsTrimeresurusTrypsinAmino Acid SequenceCysteineDisulfidesCloning MolecularMolecular BiologyPeptide sequenceMessenger RNABase SequencebiologyCell BiologyMolecular biologyRecombinant ProteinsOpen reading frameMutagenesis Site-Directedbiology.proteinJournal of Biological Chemistry
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Structure-Activity Relationships and X-ray Structures Describing the Selectivity of Aminopyrazole Inhibitors for c-Jun N-terminal Kinase 3 (JNK3) ove…

2009

c-Jun N-terminal kinase 3alpha1 (JNK3alpha1) is a mitogen-activated protein kinase family member expressed primarily in the brain that phosphorylates protein transcription factors, including c-Jun and activating transcription factor-2 (ATF-2) upon activation by a variety of stress-based stimuli. In this study, we set out to design JNK3-selective inhibitors that had >1000-fold selectivity over p38, another closely related mitogen-activated protein kinase family member. To do this we employed traditional medicinal chemistry principles coupled with structure-based drug design. Inhibitors from the aminopyrazole class, such as SR-3576, were found to be very potent JNK3 inhibitors (IC(50) = 7 nm)…

Models MolecularStereochemistryProtein ConformationPyrazoleCrystallography X-RayBiochemistryp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundStructure-Activity RelationshipProtein structureMitogen-Activated Protein Kinase 10Insulin-Secreting CellsStructure–activity relationshipAnimalsHumansEnzyme InhibitorsPhosphorylationProtein kinase AMolecular BiologyCells CulturedIndazolebiologyActivating Transcription Factor 2Active siteCell BiologyActivating transcription factor 2RatschemistryProtein Structure and Foldingbiology.proteinPyrazolesSelectivityJournal of Biological Chemistry
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The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

2006

Abstract The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ∼2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler–type reaction and represents a novel…

Models MolecularTryptamineProtein FoldingStrictosidine synthaseProtein ConformationMolecular Sequence DataSequence alignmentPlant ScienceCatalysisRauwolfiaSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaCarbon-Nitrogen LyasesAmino Acid SequenceResearch ArticlesConserved SequencePlant ProteinsBinding SitesSequence Homology Amino AcidbiologyIndole alkaloidActive siteCell BiologyLyasebiology.organism_classificationTryptamineschemistryBiochemistrybiology.proteinSecologaninSequence AlignmentThe Plant Cell
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Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.

2015

Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disp…

Models MolecularVesicle-associated membrane protein 8Protein FoldingTRPV5Protein ConformationBiophysicsTRPV Cation ChannelsBiochemistryTRPVTransient receptor potential channelAnimalsHumansProtein Structure QuaternaryMolecular BiologyIon channelTransmembrane channelsChemistryCell MembraneCell BiologyTransmembrane proteinRecombinant ProteinsAnkyrin RepeatProtein Structure TertiaryRatsHEK293 CellsBiochemistryBiophysicsAnkyrin repeatBiochemical and biophysical research communications
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