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Molecules 2011, 16(9), 7909-7935; doi:10.3390/molecules16097909
Review

Pyrene: A Probe to Study Protein Conformation and Conformational Changes

1, 1 and 1,2,*
Received: 1 August 2011 / Revised: 4 September 2011 / Accepted: 6 September 2011 / Published: 14 September 2011
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Abstract

The review focuses on the unique spectral features of pyrene that can be utilized to investigate protein structure and conformation. Pyrene is a fluorescent probe that can be attached covalently to protein side chains, such as sulfhydryl groups. The spectral features of pyrene are exquisitely sensitive to the microenvironment of the probe: it exhibits an ensemble of monomer fluorescence emission peaks that report on the polarity of the probe microenvironment, and an additional band at longer wavelengths, the appearance of which reflects the presence of another pyrene molecule in spatial proximity (~10 Å). Its high extinction coefficient allows us to study labeled proteins in solution at physiologically relevant concentrations. The environmentally- and spatially-sensitive features of pyrene allow monitoring protein conformation, conformational changes, protein folding and unfolding, protein-protein, protein-lipid and protein-membrane interactions.
Keywords: pyrene; excimer; monomer; Py value; apolipoproteins; fluorescence; protein oligomerization; protein-lipid interactions; protein-membrane interactions pyrene; excimer; monomer; Py value; apolipoproteins; fluorescence; protein oligomerization; protein-lipid interactions; protein-membrane interactions
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Bains, G.; Patel, A.B.; Narayanaswami, V. Pyrene: A Probe to Study Protein Conformation and Conformational Changes. Molecules 2011, 16, 7909-7935.

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