Search results for "Biophysic"

showing 10 items of 3565 documents

New Insights into Protein (Un)Folding Dynamics.

2015

A fundamental open problem in biophysics is how the folded structure of the main chain (MC) of a protein is determined by the physics of the interactions between the side-chains (SCs). All-atom molecular dynamics simulations of a model protein (Trp-cage) revealed that strong correlations between the motions of the SCs and the MC occur transiently at 380 K in unfolded segments of the protein, and during the simulations of the whole amino-acid sequence at 450 K. The high correlation between the SC and MC fluctuations is a fundamental property of the unfolded state and is also relevant to unstructured proteins as Intrinsically Disordered Proteins (IDPs), for which new reaction coordinates are …

Protein FoldingChemistryOpen problemBiophysicsProteinsSequence (biology)Molecular Dynamics SimulationIntrinsically disordered proteinsArticleFolding (chemistry)Intrinsically Disordered ProteinsCrystallographyMolecular dynamicsSide chainBiophysicsHumansThermodynamicsGeneral Materials ScienceProtein foldingAmino Acid SequencePhysical and Theoretical ChemistryPeptidesPeptide sequenceThe journal of physical chemistry letters
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Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics

2015

Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native neuroserpin and its dysfunctional conformation isoforms: the proteolytically cleaved conformer, the inactive latent conformer, and the polymeric species. Based on circular dichroism and fluorescence spectroscopy, we present an experimental validation of the latent model and highlight the main structural features of the different conformers. In particular, emission spectra of aromatic res…

Protein FoldingCircular dichroismSerine Proteinase InhibitorsProtein ConformationStereochemistryNeuroserpinBiophysicsEpilepsies MyoclonicMolecular Dynamics SimulationSerpinMolecular DynamicsBiochemistryProtein Structure SecondaryArticleFluorescenceAnalytical ChemistryMolecular dynamicsProtein structureNeuroserpinmedicineHumansProtein IsoformsFluorescence emission spectra; circular dichroism; neuroserpin latent conformationneuroserpin latent conformationFamilial encephalopathy with neuroserpin inclusion bodiesMolecular BiologyConformational isomerismSerpinsFluorescence emission spectraSerpinChemistryCircular DichroismConformational diseaseNeuropeptidesHydrogen Bondingmedicine.diseaseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Heredodegenerative Disorders Nervous SystemProtein foldingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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The production of 85 kDa N-terminal fragment of apolipoprotein B in mutant HepG2 cells generated by targeted modification of apoB gene occurs by ALLN…

2010

Abstract To study the mechanism of low levels of full length and truncated apoB in individuals heterozygous for apoB truncation, a non-sense mutation was introduced in one of the three alleles of apob gene of HepG2 cells by homologous recombination. Despite very low levels of apoB-82 (1–2%) in the media, a prominent N-terminal apoB protein of 85 kDa (apoB-15) was secreted that fractionated at d > 1.065 in density gradient ultracentrifugation. The mechanism of production of this short protein was studied by 35S-methionine pulse–chase experiment. Oleate prevented presecretory degradation of apoB-100 in the cell and resulted in increased secretion of newly synthesized apoB-100 with decreases i…

Protein FoldingHepG2Apolipoprotein BLeupeptinsmedicine.medical_treatmentMutantBiophysicsBiologyCysteine Proteinase Inhibitorsdigestive systemBiochemistry85 kDa N-terminalCysteine ProteasesapoBmedicineHumansSecretionMolecular BiologyApolipoproteins BProteasenutritional and metabolic diseasesCell BiologyHep G2 CellsCysteine proteaseMolecular biologyTransmembrane proteinProtein TransportCodon NonsenseHypobetalipoproteinemia Familial Apolipoprotein Bbiology.proteinlipids (amino acids peptides and proteins)Density gradient ultracentrifugationIntracellular
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The membrane environment modulates self-association of the human GpA TM domain--implications for membrane protein folding and transmembrane signaling.

2010

Abstract The influence of lipid bilayer properties on a defined and sequence-specific transmembrane helix–helix interaction is not well characterized yet. To study the potential impact of changing bilayer properties on a sequence-specific transmembrane helix–helix interaction, we have traced the association of fluorescent-labeled glycophorin A transmembrane peptides by fluorescence spectroscopy in model membranes with varying lipid compositions. The observed changes of the glycophorin A dimerization propensities in different lipid bilayers suggest that the lipid bilayer thickness severely influences the monomer–dimer equilibrium of this transmembrane domain, and dimerization was most effici…

Protein FoldingLipid BilayersMolecular Sequence DataBiophysicsGpABiochemistryFluorescenceMembrane LipidsOrientations of Proteins in Membranes databaseMembrane fluidityFluorescence Resonance Energy TransferHumansAmino Acid SequenceGlycophorinsBilayerLipid bilayerIntegral membrane proteinBinding SitesChemistryBilayerPeripheral membrane proteinTemperatureMembrane ProteinsCell BiologyTransmembrane proteinCell biologyTransmembrane domainCholesterolSpectrometry FluorescenceFRETPhosphatidylcholineslipids (amino acids peptides and proteins)Transmembrane helix–helix interactionProtein MultimerizationPeptidesHydrophobic and Hydrophilic InteractionsSignal TransductionBiochimica et biophysica acta
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Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.

2019

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+ -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore…

Protein FoldingProtein ConformationLipoproteinsBiophysicsBiochemistryMicrobiology03 medical and health sciencesLyme diseaseBacterial ProteinsStructural BiologyOxidoreductaseGeneticsmedicineHumansBinding siteBorrelia burgdorferiMolecular BiologyFerredoxin030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseaseBinding SitesbiologyChemistry030302 biochemistry & molecular biologyCell BiologyPeriplasmic spacebacterial infections and mycosesmedicine.diseasebiology.organism_classificationZincMembrane proteinBorrelia burgdorferiPeriplasmbacteriaNAD+ kinaseSodium-Potassium-Exchanging ATPaseFEBS lettersReferences
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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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Self-assembly of biopolymeric structures below the threshold of random cross-link percolation

1996

Self-assembly of extended structures via cross-linking of individual biomolecules often occurs in solutions at concentrations well below the estimated threshold for random cross-link percolation. This requires solute-solute correlations. Here we study bovine serum albumin. Its unfolding causes the appearance of an instability region of the sol, not observed for native bovine serum albumin. As a consequence, spinodal demixing of the sol is observed. The thermodynamic phase transition corresponding to this demixing is the determinative symmetry-breaking step allowing the subsequent occurrence of (correlated) cross-linking and its progress up to the topological phase transition of gelation. Th…

Protein FoldingSpinodalPhase transitionProtein ConformationBiophysicsIn Vitro TechniquesInstabilityBiophysical PhenomenaBiopolymersDrug StabilityAnimalsTopological orderBovine serum albuminQuantitative Biology::BiomoleculesMolecular StructurebiologyChemistrySerum Albumin BovineCrystallographyCross-Linking ReagentsChemical physicsPercolationbiology.proteinThermodynamicsCattleProtein foldingSelf-assemblyGelsResearch Article
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Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia

2019

Mitral valve diseases affect approximately 3% of the population and are the most common reasons for valvular surgery because no drug-based treatments exist. Inheritable genetic mutations have now been established as the cause of mitral valve insufficiency, and four different missense mutations in the filamin A gene (FLNA) have been found in patients suffering from non-syndromic mitral valve dysplasia (MVD). The FLNA protein is expressed, in particular, in endocardial endothelia during fetal valve morphogenesis and is key in cardiac development. The FLNA-MVD causing mutations are clustered in the N-terminal region of FLNA. How the mutations in FLNA modify its structure and function, have mos…

Protein FoldingdysplasiatFilamins[SDV]Life Sciences [q-bio]PopulationProtein Tyrosine Phosphatase Non-Receptor Type 12BiophysicsMutation Missensesynnynnäiset sydänviatProtein tyrosine phosphataseBiologyMolecular Dynamics Simulationmedicine.disease_causeFilamin03 medical and health sciences0302 clinical medicinemitral valve dysplasiaMitral valvemedicineFLNAMissense mutationHumanseducationGene030304 developmental biologyGenetics0303 health sciencesMutationeducation.field_of_studyBinding SitesMitral Valve Prolapsecritical structural defectshiippaläppäfilamiinitArticles3. Good healthmedicine.anatomical_structurecardiovascular systemfilamin A mutationsgeneettiset tekijätmutaatiot030217 neurology & neurosurgeryProtein Binding
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Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

2012

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM domain of the model membrane protein glycophorin A (GpA), we address the consequences of replacing specific residues by ionizable amino acids on TM helix insertion and packing, both in detergent micelles and in biological membranes. Our findings demonstrate that ionizable residues are stably inserted in hydrophobic environments, and tolerated in t…

Protein Foldinglcsh:MedicineBiochemistryBiotecnologiaProtein Structure SecondaryCell membraneGlycophorinsAmino Acidslcsh:ScienceMicelleschemistry.chemical_classificationMultidisciplinarybiologySodium Dodecyl SulfateLipidsTransmembrane proteinAmino acidmedicine.anatomical_structureBiochemistryCytochemistryThermodynamicsResearch ArticleProtein StructureBiophysicsCalcium-Transporting ATPasesProtein ChemistryProtein–protein interactionMembranes (Biologia)MicrosomesEscherichia colimedicineGlycophorinProtein InteractionsBiologyCell Membranelcsh:RMembrane ProteinsProteinsComputational BiologyBiological membraneIntracellular MembranesProtein Structure TertiaryTransmembrane ProteinsMembrane proteinchemistryHelixbiology.proteinBiophysicslcsh:QProtein Multimerization
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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