Giudici, A MarcelaHernandez-Cifre, Jose GCamara-Artigas, AnaHornos, FelipeMartinez-Rodriguez, SergioCarlos Alvarez-Perez, JuanDiaz-Cano, InesEsther Farez-Vidal, MariaNeira, Jose L2023-02-092023-02-092020-06-30Giudici AM, Hernández-Cifre JG, Cámara-Artigas A, Hornos F, Martínez-Rodríguez S, Carlos Alvarez-Pérez J, et al. The isolated armadillo-repeat domain of Plakophilin 1 is a monomer in solution with a low conformational stability. J Struct Biol. 2020 Sep 1;211(3):107569.http://hdl.handle.net/10668/15918Plakophilin 1 (PKP1) is a member of the armadillo repeat family of proteins. It serves as a scaffold component of desmosomes, which are key structural components for cell-cell adhesion. We have embarked on the biophysical and conformational characterization of the ARM domain of PKP1 (ARM-PKP1) in solution by using several spectroscopic (namely, fluorescence and circular dichroism (CD)) and biophysical techniques (namely, analytical ultracentrifugation (AUC), dynamic light scattering (DLS) and differential scanning calorimetry (DSC)). ARM-PKP1 was a monomer in solution at physiological pH, with a low conformational stability, as concluded from DSC experiments and thermal denaturations followed by fluorescence and CD. The presence or absence of disulphide bridges did not affect its low stability. The protein unfolded through an intermediate which has lost native-like secondary structure. ARM-PKP1 acquired a native-like structure in a narrow pH range (between pH 6.0 and 8.0), indicating that its adherent properties might only work in a very narrow pH range.enAnalytical ultracentrifugationCircular dichroismConformational stabilityDifferential scanning calorimetryFluorescenceScatteringAnilino NaphthalenesulfonatesCalorimetry, Differential ScanningCircular DichroismDynamic Light ScatteringHumansHydrogen-Ion ConcentrationPlakophilinsProtein ConformationProtein DenaturationProtein DomainsSolutionsSpectrometry, FluorescenceUltracentrifugationThe isolated armadillo-repeat domain of Plakophilin 1 is a monomer in solution with a low conformational stability.research article32650131Restricted AccessConcentración de iones de HidrógenoConformación proteicaDesnaturalización proteicaDicroismo circularDispersión dinámica de luzDominios proteicosEspectrometría de fluorescencia humanosNaftalenosulfonatos de anilina placofilinasRastreo diferencial de calorimetríaSoluciones ultracentrifugación10.1016/j.jsb.2020.1075691095-8657http://hdl.handle.net/10261/235776