pyrene a probe to study protein conformation and conformational changes芘探针来研究蛋白质构象和构象变化.pdfVIP

Molecules 2011, 16, 7909-7935; doi:10.3390/molecule OPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Review Pyrene: A Probe to Study Protein Conformation and Conformational Changes Gursharan Bains 1, Arti B. Patel 1 and Vasanthy Narayanaswami 1,2,* 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; E-Mail: vnaraya2@; Tel.: +1-562-985-4953; Fax: +1-562-985-8557. Received: 1 August 2011; in revised form: 4 SeReceived: 1 August 2011; in revised from: 4 September 2011 / Accepted: 6 September 2011 / Published: 14 September 2011Published: 13 September 2011 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