Search results for "free energy calculations"

showing 2 items of 2 documents

An omics perspective to the molecular mechanisms of anticancer metallo-drugs in the computational microscope era

2017

Introduction: Metallo-drugs have attracted enormous interest for cancer treatment. The achievements of this drug-type are summarized by the success story of cisplatin. That being said, there have been many drawbacks with its clinical use, which prompted decades worth of research efforts to move towards safer and more effective agents, either containing platinum or different metals. Areas covered: In this review, the authors provide an atomistic picture of the molecular mechanisms involving selected metallo-drugs from structural and molecular simulation studies. They also provide an omics perspective, pointing out many unsettled aspects of the most relevant families of metallo-drugs at an ep…

Computer scienceAntineoplastic AgentsNanotechnologyMolecular simulation010402 general chemistryQM/MM01 natural sciencesmetadynamicsEpigenesis Geneticmetallo-drugNeoplasmsDrug DiscoveryHumansComputer SimulationplatinumrutheniumSettore CHIM/03 - Chimica Generale e InorganicaG-quadruplex010405 organic chemistryNAMI-AnucleosomePerspective (graphical)free energy calculationsDNAData sciencemolecular dynamics0104 chemical sciencesCancer treatmentMetalscopperDrug DesignComputer-Aided DesignCisplatinExpert Opinion on Drug Discovery
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Why Are Some Enzymes Dimers? Flexibility and Catalysis in Thermotoga maritima Dihydrofolate Reductase

2019

[Image: see text] Dihydrofolate reductase from Thermotoga maritima (TmDFHFR) is a dimeric thermophilic enzyme that catalyzes the hydride transfer from the cofactor NADPH to dihydrofolate less efficiently than other DHFR enzymes, such as the mesophilic analogue Escherichia coli DHFR (EcDHFR). Using QM/MM potentials, we show that the reduced catalytic efficiency of TmDHFR is most likely due to differences in the amino acid sequence that stabilize the M20 loop in an open conformation, which prevents the formation of some interactions in the transition state and increases the number of water molecules in the active site. However, dimerization provides two advantages to the thermophilic enzyme: …

chemistry.chemical_classificationenzyme kinetic isotope effectsbiology010405 organic chemistryStereochemistryChemistryThermophilefree energy calculationsGeneral Chemistry010402 general chemistrybiology.organism_classificationenzyme dimers01 natural sciencesCatalysisCofactor0104 chemical sciencesCatalysisEnzymeDihydrofolate ReductaseThermotoga maritimaDihydrofolate reductasebiology.proteinbacteriaQM/MM methods
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