By Richard N. Day, Michael W. Davidson
Advances in fluorescent proteins, live-cell imaging, and superresolution instrumentation have ushered in a brand new period of investigations in cellphone biology, medication, and body structure. From the id of the fairway fluorescent protein within the jellyfish Aequorea victoria to the engineering of novel fluorescent proteins, The Fluorescent Protein Revolution explores the background, homes, and purposes of those very important probes.
The e-book first lines the background of fluorescent proteins and the revolution they enabled in mobile imaging. It then discusses fluorescent proteins with novel photophysical homes. The e-book additionally covers a number of state-of-the-art imaging functions. those comprise superresolution microscopy of mobile high quality constructions, be concerned microscopy to imagine protein interactions and cell-signaling actions within residing cells, photobleaching and photoactivation suggestions to imagine protein behaviors, ideas that make the most plant and algal photoreceptors to permit light-regulated keep watch over of enzymatic actions, and the noninvasive imaging of tumor–host interactions in dwelling animals.
In colour all through, this booklet offers the basic rules and most up-to-date advances within the box, together with the linked improvement of imaging recommendations that make the most fluorescent proteins. it's available to a vast viewers, from optical imaging specialists to newcomers desiring an creation to the field.
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Extra resources for The Fluorescent Protein Revolution
Prasher. 1994. Green fluorescent protein as a marker for gene expression. Science 263:802–805. A. V. Matz. 2005. Applications of ancestral protein reconstruction in understanding protein function: GFP-like proteins. In Molecular Evolution: Producing the Biochemical Data, Part B, eds. A. Zimmer and E. , Waltham, MA: Academic Press. , A. Diaspro, F. Cannone, M. Collini, S. Bologna, V. Pellegrini, and F. Beltram. 2005. Selective fluorescence recovery after bleaching of single E(2)GFP proteins induced by twophoton excitation.
The all-atom representation is a nearly perfect cylinder about 25 Ǻ wide and 40 Ǻ tall. 1b) shows that the structure can be conceptually divided into sequential segments, for example, an N-terminal portion (roughly residues 1–80) consisting of three beta strands plus the central helix and a larger C-terminal portion (roughly residues 81–238) that consists of eight beta strands arranged in a “Greek key” motif. This formal compartmentalization helps to understand the initially surprising observation that GFP, despite its monolithic appearance, can be expressed as two separate segments that combine within cells to yield a functional FP (Ghosh et al.
Oswald, K. Nienhaus, K. Deuschle, C. Roecker, M. Wolff, R. Heilker, G. Ulrich Nienhaus, and J. Wiedenmann. 2009. mRuby, a bright monomeric red fluorescent protein for labeling of subcellular structures. PLoS One 4 (2):e4391. , F. Dimler, G. Jung, and T. Brixner. 2009. Ultrafast photoconversion of the green fluorescent protein studied by accumulative femtosecond spectroscopy. Biophysical Journal 96:2763–2770. L. R. Meech. 2004. Observation of low frequency vibrational modes in a mutant of the green fluorescent protein.