63 research outputs found
βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions
β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous work demonstrated that dimerization of both βA3 and βB2 crystallins (βA3 and βB2) involves endothermic enthalpy of association (âź8 kcal/mol) mediated by hydrophobic interactions.Thermodynamic profiles of the associations of dimeric βA3 and βB1 and tetrameric βB1/βA3 were measured using sedimentation equilibrium. The homo- and heteromolecular associations of βB1 crystallin are dominated by exothermic enthalpy (-13.3 and -24.5 kcal/mol, respectively).Global thermodynamics of βB1 interactions suggest a role in the formation of stable protein complexes in the lens via specific van der Waals contacts, hydrogen bonds and salt bridges whereas those β-crystallins which associate by predominately hydrophobic forces participate in a weaker protein associations
Learning about âcauseâ and âeffectâ through well-designed studies of air quality interventions
Estimating the palliative effect of percutaneous endoscopic gastrostomy in an observational registry using principal stratification and generalized propensity scores
1H-NMR spectroscopy shows cellular uptake of HEPES buffer by human cell linesâan effect to be considered in cell culture experiments
Non-thermal atmospheric pressure plasmas as a novel candidate for preventive therapy of melanoma
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