Pyrene: A Probe to Study Protein Conformation and Conformational ChangesReport as inadecuate




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1

Department of Chemistry and Biochemistry, 1250 Bellflower Boulevard, California State University Long Beach, Long Beach, CA 90840, USA

2

Children’s Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, USA





*

Author to whom correspondence should be addressed.



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





Author: Gursharan Bains 1, Arti B. Patel 1 and Vasanthy Narayanaswami 1,2,*

Source: http://mdpi.com/



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