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A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin

Paper ID Volume ID Publish Year Pages File Format Full-Text
31021 44529 2010 9 PDF Available
Title
A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin
Abstract

UV–vis, time-resolved fluorescence and circular dichroism spectroscopic investigations have been made to reveal the nature of the interactions between xanthene dye Rhodamine 6G and the well known protein hemoglobin. From the analysis of the steady-state and time-resolved fluorescence quenching of Rhodamine 6G in aqueous solutions in presence of hemoglobin, it is revealed that the quenching is static in nature. The primary binding pattern between Rhodamine and hemoglobin has been interpreted as combined effect of hydrophobic association and electrostatic interaction. The binding constants, number of binding sites and thermodynamic parameters at various pH of the environment have been computed. The binding average distance between the energy donor Rhodamine and acceptor hemoglobin has been determined from the Forster’s theory.

Keywords
Time resolved spectroscopy; Circular dichroism; Rhodamine 6G; Hemoglobin; Static quenching; Hydrophobic interactions
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A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 99, Issue 2, 3 May 2010, Pages 78–86
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us