Search results for "Stability"

showing 10 items of 3085 documents

Efficient computation of root mean square deviations under rigid transformations

2013

The computation of root mean square deviations (RMSD) is an important step in many bioinformatics applications. If approached naively, each RMSD computation takes time linear in the number of atoms. In addition, a careful implementation is required to achieve numerical stability, which further increases runtimes. In practice, the structural variations under consideration are often induced by rigid transformations of the protein, or are at least dominated by a rigid component. In this work, we show how RMSD values resulting from rigid transformations can be computed in constant time from the protein's covariance matrix, which can be precomputed in linear time. As a typical application scenar…

Protein ConformationCovariance matrixComputationComputational BiologyProteinsGeometryGeneral ChemistryRoot mean squareComputational MathematicsComputer SimulationStatistical physicsCluster analysisConstant (mathematics)Time complexityRigid transformationMathematicsNumerical stabilityJournal of Computational Chemistry
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The Closed/Open Model for Lipase Activation. Addressing Intermediate Active Forms of Fungal Enzymes by Trapping of Conformers in Water-Restricted Env…

2001

The behavior of prototypic fungal lipases in a water-restricted environment has been investigated by exploiting the reported experimental strategy that allows the trapping (freeze-drying) of the enzyme in the conformation present in aqueous solution and to subsequently assay it in nonaqueous media [Mingarro, I., Abad, C., and Braco, L. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 3308-3312]. We now report, using simple esterification as well as acidolysis (triglycerides as substrates) as nonaqueous model reactions, that the presence of a detergent (n-octyl-beta-glucopyranoside) in the freeze-drying buffer, at concentrations below the critical micellar concentration, generates different catalyti…

Protein ConformationStereochemistryThioglucosidesDetergentsTrappingBuffersBiochemistryFungal ProteinsAscomycotaEnzyme StabilityMoleculeLipaseConformational isomerismMicellesTriglyceridesCandidachemistry.chemical_classificationAqueous solutionbiologyWaterLipaseGeotrichumEnzyme ActivationSolutionsFreeze DryingEnzymeModels ChemicalchemistryCritical micelle concentrationbiology.proteinFungal enzymesRhizopusBiochemistry
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Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin

2004

Hemocyanin sequences allineament shows the presence of highly invariant regions especially in the active site and in the tight intersubunits interaction sites. Comparing the aminoacids in contact regions between monomers is possible to interpret the stability of hexamers.

Protein Conformationmedicine.medical_treatmentGeneral Physics and AstronomyBiologyPenaeus monodon03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePenaeidaeStructural BiologymedicineAnimalsGeneral Materials Science030304 developmental biology0303 health sciencesEcologyActive siteHemocyaninCell Biologybiology.organism_classificationOxygenMonomerchemistryHemocyaninsBiophysicsbiology.proteinProtein quaternary structureConformational stability030217 neurology & neurosurgeryOxygen binding
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Biotechnical applications of small heat shock proteins from bacteria.

2012

The stress responses of most bacteria are thought to involve the upregulation of small heat shock proteins. We describe here some of the most pertinent aspects of small heat shock proteins, to highlight their potential for use in various applications. Bacterial species have between one and 13 genes encoding small heat shock proteins, the precise number depending on the species considered. Major efforts have recently been made to characterize the protein protection and membrane stabilization mechanisms involving small heat shock proteins in bacteria. These proteins seem to be involved in the acquisition of cellular heat tolerance. They could therefore potentially be used to maintain cell via…

Protein FoldingHeterologousmedicine.disease_causeBiochemistryMicrobiologyDownregulation and upregulationBacterial ProteinsStress PhysiologicalHeat shock proteinmedicineHumansViability assayEscherichia coliInclusion BodiesbiologyProtein StabilityProbioticsCell Biologybiology.organism_classificationRecombinant ProteinsCell biologyHeat-Shock Proteins SmallSolubilityShock (circulatory)Food TechnologyProtein foldingmedicine.symptomBacteriaBiotechnologyThe international journal of biochemistrycell biology
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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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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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Atomic mean square displacements in proteins by Molecular Dynamics: a case for analysis of variance

2004

Information on protein internal motions is usually obtained through the analysis of atomic mean-square displacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach to analyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a technique inspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze them statistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzyme and a mesophilic homolog. In agreement with previous experimental observations, …

Proteins Protein Stabilitythermophilic proteins
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Human apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity

2012

Human apolipoprotein A-I (apoA-I)-derived amyloidosis can present with either wild-type (Wt) protein deposits in atherosclerotic plaques or as a hereditary form in which apoA-I variants deposit causing multiple organ failure. More than 15 single amino acid replacement amyloidogenic apoA-I variants have been described, but the molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here, we have investigated by fluorescence and biochemical approaches the stabilities and propensities to aggregate of two disease-associated apoA-I variants, apoA-IGly26Arg, associated with polyneuropathy and kidney dysfunction, and apoA-ILys107-0, implicated in amyloidosis in severe…

ProteomicsProtein Foldinglcsh:MedicineProtein aggregationpolymyxinsBiochemistryProtein Structure SecondaryMiceProtein structureneutrophilsMolecular Cell Biologypolycyclic compoundslcsh:ScienceCellular Stress ResponsesMultidisciplinaryProtein StabilityAmyloidosisCiencias QuímicasfluorescenseCell biologymacrophagesBiochemistryToxicityMedicineProtein foldinglipids (amino acids peptides and proteins)medicine.symptomPolyneuropathyResearch ArticleProtein StructureMedicinaLipoproteinsImmunologyBiophysicsInflammationAmyloidogenic ProteinsBiologyProtein ChemistryMicrobiologyCell Lineprotein aggregationmacrophage activationmedicineAnimalsHumansoligomersProtein InteractionsBiologyInflammationamyloidosisApolipoprotein A-IMacrophageslcsh:RImmunityProteinsnutritional and metabolic diseasesmedicine.diseaseApolipoproteinsAmino Acid SubstitutionCell cultureinflammationCiencias Médicaslcsh:QClinical ImmunologyMutant ProteinspolyneuropathyProtein Multimerization
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Irinotecan or oxaliplatin: Which is the first move for the mate?

2020

Objectives: The aim of the present review is to discuss the potential link between RAS, BRAF and microsatellite instability (MSI) mutational patterns and chemotherapeutic agent efficacy [Irinotecan (IRI) vs. Oxaliplatin (OXA)], and how this can potentially influence the choice of the chemotherapy backbone. Methods: Following a review of the research literature, all pertinent articles published in the core journals were selected for the study. The inclusion criteria regarded relevant clinical and pre-clinical studies on the topic of interest (Relationship of OXA and IRI to KRAS/BRAF mutations and MSI). Results: Excision repair cross complementation group 1 (ERCC1) expression is inhibited by…

Proto-Oncogene Proteins B-rafColorectal cancerPopulationmedicine.disease_causeIrinotecanBiochemistryDNA Mismatch RepairSettore MED/06BRAFDrug DiscoveryKRASMedicineChemotherapyHumanseducationMSIPharmacologyeducation.field_of_studybusiness.industryOrganic ChemistryMicrosatellite instabilitymedicine.diseaseColorectal cancerdigestive system diseasesOxaliplatinIrinotecanOxaliplatinGenes rasMutationCancer researchMolecular MedicineMolecular targetsDNA mismatch repairMicrosatellite InstabilityKRASERCC1businessColorectal Neoplasmsmedicine.drug
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Understanding the clinical behavior of relapsed colon cancers with microsatellite instability relative to BRAF mutations

2019

Background Microsatellite instable/deficient mismatch repair (MSI/dMMR) metastatic colorectal cancers have been reported to have a poor prognosis. Frequent co-occurrence of MSI/dMMR and BRAFV600E complicates the association. Patients and methods Patients with resected stage III colon cancer (CC) from seven adjuvant studies with available data for disease recurrence and MMR and BRAFV600E status were analyzed. The primary end point was survival after recurrence (SAR). Associations of markers with SAR were analyzed using Cox proportional hazards models adjusted for age, gender, performance status, T stage, N stage, primary tumor location, grade, KRAS status, and timing of recurrence. Results A…

Proto-Oncogene Proteins B-rafdeficient mismatch repairrecurrenceBrain Neoplasmsbusiness.industryGastrointestinal tumorMicrosatellite instabilityHematologyPrognosismedicine.diseasedigestive system diseasesText miningcolon cancerOncologyNeoplastic Syndromes HereditaryColonic NeoplasmsmedicineCancer researchHumansmicrosatellite instabilityNeoplasm Recurrence LocalColorectal NeoplasmsbusinessAnnals of Oncology
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