Search results for "Mutant Protein"

showing 2 items of 42 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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Active site conformation in the αH87G mutant hemoglobin: An optical absorption and FTIR study

2000

We have studied the active site conformation in the carbonmonoxy derivative of the αH87G mutant hemoglobin by means of optical absorption and FTIR spectroscopies. A red shift (≈30 cm−1) of the Soret band peak frequency, together with a concomitant red shift (≈2 cm−1) of the bound CO stretching frequency has been observed for the mutant protein. This indicates an altered electrostatic environment of the heme group in the mutated subunits. In view of the FTIR data showing that the bound CO molecule experiences an increased positive electrostatic field, we attribute the observed effects to a closer interaction of the CO ligand with the partially positively charged imidazole side chain of the p…

biologyAnalytical chemistryActive siteLigand (biochemistry)chemistry.chemical_compoundCrystallographychemistryMutant proteinbiology.proteinSide chainImidazoleHemoglobinHemeHistidineAIP Conference Proceedings
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