Spectroscopic Investigation of the Structure of a Protein Adsorbed on a Hydrophobic Latex |
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Authors: | Marc C. L. Maste Everard H. W. Pap Arie van Hoek Willem Norde Antonie J. W. G. Visser |
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Affiliation: | aDepartment of Physical and Colloid Chemistry, P.O. Box 8038, 6700 EK, Wageningen, The Netherlands;bDepartment of Biochemistry, Wageningen Agricultural University, The Netherlands;cDepartment of Molecular Physics, Wageningen Agricultural University, The Netherlands |
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Abstract: | Spectroscopic methods provide a powerful tool for investigating the structural properties of immobilized proteins. For that purpose, there was a strong need for a hydrophobic particle that allows determination of the adsorbed protein conformation by fluorescence and circular dichroism. Among the various hydrophobic suspensions that are available, perfluoro-alkoxy fluoro carbon Teflon latex satisfies the requirements of low light absorption and scattering. As an example, preliminary results of structural changes of a proteolytic enzyme dissolved in aqueous solution and in the adsorbed state are given. |
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Keywords: | protein adsorption hydrophobic particle fluorescence circular dichroism |
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