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Our understanding of molecular chaperone function in membrane protein biogenesis lags far behind that in soluble protein biogenesis. Through a combined approach including isothermal titration calorimetry, UV–Vis spectroscopy, and fluorescence spectroscopy, the behavior of ATP-dependent chaperonin GroEL–GroES, a paradigmatic chaperone of soluble protein folding, was investigated in the refolding of...
The adsorption of recombinant barnacle proteins Bacp19k and Mrcp19k on hydrophilic silica surface was characterized by spectroscopic ellipsometry in artificial seawater (pH=8.2). They are homologous adhesive proteins destined for underwater adhesion but bear opposite net charges in seawater. As assessed with their primary and secondary structures, both proteins are intrinsically disordered and thus...
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