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  • Title: Conformational changes of bovine serum albumin upon its adsorption in dodecane-in-water emulsions as revealed by front-face steady-state fluorescence.
    Author: Castelain C, Genot C.
    Journal: Biochim Biophys Acta; 1994 Jan 05; 1199(1):59-64. PubMed ID: 8280754.
    Abstract:
    Front-face fluorescence spectroscopy was used to characterise dodecane-in-buffer (0.1 M phosphate buffer; pH = 7.6) emulsions stabilised by bovine serum albumin (BSA). A 15-nm blue-shift of the emission maximum of the adsorbed protein and a significant increase of its fluorescence quantum yield were observed. The contribution of tyrosyl residues to total fluorescence was tentatively evaluated from different spectra and an R ratio taking into account the stray-light interference; R increased upon BSA absorption but the Tyrosine contribution remained weak in all cases. Thus, conformational changes of the protein take place upon BSA adsorption onto the dodecane-water interface. They involve modifications in the environment of the protein aromatic amino acids especially of the tryptophanyl residues which are displaced to a more hydrophobic location. Moreover, the proportions of absorbed and non-adsorbed BSA in emulsions can be estimated from the position of the emission maximum.
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