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Pyrene: A Probe to Study Protein Conformation and Conformational Changes

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 sensit...

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Detalles Bibliográficos
Autores principales: Bains, Gursharan, Patel, Arti B., Narayanaswami, Vasanthy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264589/
https://www.ncbi.nlm.nih.gov/pubmed/22143550
http://dx.doi.org/10.3390/molecules16097909
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author Bains, Gursharan
Patel, Arti B.
Narayanaswami, Vasanthy
author_facet Bains, Gursharan
Patel, Arti B.
Narayanaswami, Vasanthy
author_sort Bains, Gursharan
collection PubMed
description 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.
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spelling pubmed-62645892018-12-10 Pyrene: A Probe to Study Protein Conformation and Conformational Changes Bains, Gursharan Patel, Arti B. Narayanaswami, Vasanthy Molecules Review 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. MDPI 2011-09-14 /pmc/articles/PMC6264589/ /pubmed/22143550 http://dx.doi.org/10.3390/molecules16097909 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Bains, Gursharan
Patel, Arti B.
Narayanaswami, Vasanthy
Pyrene: A Probe to Study Protein Conformation and Conformational Changes
title Pyrene: A Probe to Study Protein Conformation and Conformational Changes
title_full Pyrene: A Probe to Study Protein Conformation and Conformational Changes
title_fullStr Pyrene: A Probe to Study Protein Conformation and Conformational Changes
title_full_unstemmed Pyrene: A Probe to Study Protein Conformation and Conformational Changes
title_short Pyrene: A Probe to Study Protein Conformation and Conformational Changes
title_sort pyrene: a probe to study protein conformation and conformational changes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264589/
https://www.ncbi.nlm.nih.gov/pubmed/22143550
http://dx.doi.org/10.3390/molecules16097909
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