Structure, Dynamics and Optical Properties of Fluorescent Proteins: Perspectives for Marker Development

Nienhaus, G. Ulrich and Wiedenmann, Jörg (2009) Structure, Dynamics and Optical Properties of Fluorescent Proteins: Perspectives for Marker Development Chemphyschem, 10, (9-10), pp. 1369-1379. (doi:10.1002/cphc.200800839).


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Fluorescent proteins of the GFP family (see picture) are key tools for life sciences research. Recent structure-dynamics-function studies have yielded new insights that aid in the rational development of advanced fluorescent marker proteins. These new markers should further extend the range of possible applications.
GFP-like proteins, originally cloned from marine animals, are genetically encoded fluorescence markers that have become indispensable tools for the life sciences. The search for GFP-like proteins with novel and improved properties is still ongoing, however, driven by the persistent need for advanced and specialized fluorescence labels for cellular imaging. Overall, the structures of these proteins are similar, but considerable variations have been found in the covalent structures and stereochemistry of the fluorophore, which govern essential optical properties such as the absorption/emission wavelengths. Moreover, as the fluorophore-enclosing cavity forms its solvation shell, it can also have a significant effect on the absorption/emission wavelengths and the brightness of the fluorophore. Most exciting are recent developments of photoactivatable fluorescence markers which change their color and/or intensity upon irradiation with light of specific wavelengths. A detailed understanding of the structure and dynamics of GFP-like proteins greatly aids in the rational engineering of advanced fluorescence marker proteins. Herein, we review our present knowledge of the structural diversity of GFP-like proteins and discuss how structure and dynamics govern their optical properties, with an emphasis on red fluorescent proteins.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1002/cphc.200800839
ISSNs: 1439-4235 (print)
Related URLs:
ePrint ID: 71848
Date :
Date Event
July 2009Published
Date Deposited: 05 Jan 2010
Last Modified: 18 Apr 2017 21:00
Further Information:Google Scholar

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