Fluorescent Proteins II: Application of Fluorescent Protein Technology (Springer Series on Fluorescence)

Fluorescent Proteins II: Application of Fluorescent Protein Technology (Springer Series on Fluorescence)

Language: English

Pages: 284

ISBN: 3642446825

Format: PDF / Kindle (mobi) / ePub

Fluorescent proteins are intimately connected to research in the life sciences. Tagging of gene products with fluorescent proteins has revolutionized all areas of biosciences, ranging from fundamental biochemistry to clinical oncology, to environmental research. The discovery of the Green Fluorescent Protein, its first, seminal application and the ingenious development of a broad palette of fluorescence proteins of other colours, was consequently recognised with the Nobel Prize for Chemistry in 2008.  

Fluorescent Proteins II highlights the physicochemical and biophysical aspects of fluorescent protein technology beyond imaging. It is tailored to meet the needs of physicists, chemists and biologists who are interested in the fundamental properties of fluorescent proteins, while also focussing on specific applications. The implementations described are cutting-edge studies and exemplify how the physical and chemical properties of fluorescent proteins can stimulate novel findings in life sciences.















excellent genetically encoded markers. The discovery of non-green GFP homologs largely expanded the application potential of the fluorescent protein technology [3–5]. In the following section, major applications of GFP-like proteins are outlined. 4.1.1 Determining Gene Activity Cell function and differentiation depend on differential gene expression [127]. Important examples of the dramatic effects of the upregulation and downregulation of genes can be found during stem cell differentiation or

increasing demand for optical tools for biomedical research. Acknowledgments J.W. acknowledges funding by the Deutsche Forschungsgemeinschaft (DFG) (grant Wi1990/2-1), the Network Fluorescence Applications in Biotechnology and Life Sciences, FABLS, Australia, the Landesstiftung Baden-W€ urttemberg (Elite Postdoc Program), the Natural Environment Research Council, UK (NE/G009643/1), and the University of Southampton. G.U.N. was supported by the DFG and the State of Baden-W€ urttemberg through the

Korzh Á D.C. Lamb Á P. Lipp Á B. Mu¨ller Á G.U. Nienhaus Á A. Pezzarossa Á T. Schmidt Á Q. Tian Á J. Wiedenmann Á T. Wohland Volume Editor Dr. Gregor Jung Professor for Biophysical Chemistry Campus B2 2 Saarland University 66123 Saarbru¨cken, Germany g.jung@mx.uni-saarland.de ISSN 1617-1306 e-ISSN 1865-1313 ISBN 978-3-642-23376-0 e-ISBN 978-3-642-23377-7 DOI 10.1007/978-3-642-23377-7 Springer Heidelberg Dordrecht London New York Library of Congress Control Number: 2011940868 # Springer-Verlag

However, the taxon anthozoa proved to be the most rewarding source for innovative fluorescent marker proteins such as red fluorescent and photoactivatable proteins [7, 9]. 2.2.2 Color Morphs The existence of several morphs with striking color differences is common among many species of reef corals and sea anemones [76–79]. Already in the nineteenth century, numerous color morphs of Anemonia sulcata (¼viridis) were described [80–82]. Five distinct color morphs of this species can be

Clomeleon and Cl-sensor exhibit relatively high sensitivity to pH (Fig. 2). Although at low [ClÀ]i (below 25 mM) the errors introduced by pH variations are relatively small (less than 10–20%), at [ClÀ]i approaching 150 mM errors may be about 50% [52]. This disadvantage has been elegantly overcome by the development of a probe allowing simultaneous recording of pH and ClÀ from the same point in space and time. 3.2.3 ClopHensor Allows Simultaneous pH and Chloride Measurements Because of the

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