Question

Extrinsic fluoresent probe for protein confomational analysis

Answer 1

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Extrinsic fluorescent dyes as tools for protein characterization

Andrea Hawe, Marc Sutter, Wim Jiskoot

Pharmaceutical research 25 (7), 1487-1499, 2008

Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, e.g. to characterize folding intermediates, measure surface hydrophobicity, and detect aggregation or fibrillation. The main underlying mechanisms, which explain the fluorescence properties of many extrinsic dyes, are solvent relaxation processes and (twisted) intramolecular charge transfer reactions, which are affected by the environment and by interactions of the dyes with proteins. In recent time, the use of extrinsic fluorescent dyes such as ANS, Bis-ANS, Nile Red, Thioflavin T and others has increased, because of their versatility, sensitivity and suitability for high-throughput screening. The intention of this review is to give an overview of available extrinsic dyes, explain their spectral properties, and show illustrative examples of their various applications in protein characterization.

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Spectroscopic probe analysis for exploring probe–protein interaction: a mapping of native, unfolding and refolding of protein bovine serum albumin by extrinsic fluorescence probe

Anuva Samanta, Bijan Kumar Paul, Nikhil Guchhait

Biophysical chemistry 156 (2-3), 128-139, 2011

Steady state and dynamic fluorescence measurements have been used to investigate interaction between Bovine Serum Albumin (BSA) and fluorescence probe para-N,N-dimethylamino orthohydroxy benzaldehyde (PDOHBA), a structurally important molecule exhibiting excited state coupled proton transfer (PT) and charge transfer (CT) reaction. Fluorescence anisotropy, acrylamide quenching, and time resolved fluorescence measurements corroborate the binding nature of the probe with protein. The binding constant between BSA and PDOHBA …