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  • Title: Dynamics surrounding Cys-34 in native, chemically denatured, and silica-adsorbed bovine serum albumin.
    Author: Wang R, Sun S, Bekos EJ, Bright FV.
    Journal: Anal Chem; 1995 Jan 01; 67(1):149-59. PubMed ID: 7864387.
    Abstract:
    We report the steady-state and time-resolved fluorescence of 6-acryloyl(dimethylamino)naphthalene (acrylodan) covalently attached to Cys-34 in bovine serum albumin (BSA). For this conceptually simple system, complicated fluorescence intensity and anisotropy decay kinetics are observed. The steady-state and time-resolved results demonstrate the presence of an excited-state reaction for the BSA-acrylodan system. Additional analysis shows that dipolar relaxation of the environment surrounding acrylodan within BSA is responsible for most of the observed time-dependent evolution of the emission spectrum. The effects of temperature, chemical denaturation, and protein adsorption to a bare silica substrate are also investigated. These results demonstrate the complexity of the changes within a protein/biorecognition element that affect the signal from a single fluorescent reporter group.
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