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By Ludwig Brand, Michael L. Johnson

The significantly acclaimed laboratory normal for greater than 40 years, Methods in Enzymology is among the so much hugely revered guides within the box of biochemistry. for the reason that 1955, each one quantity has been eagerly awaited, usually consulted, and praised through researchers and reviewers alike. greater than 270 volumes were released (all of them nonetheless in print) and lots more and plenty of the cloth is appropriate even today--truly a vital booklet for researchers in all fields of existence sciences.

Key Features
* Fluorescence in biophysics
* Fluorescence as a device for learning proteins
* choice of ground-state dissociation consistent by way of fluorescence spectroscopy
* Fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions
* Fluorescence tools for learning equilibrium macromolecule-liquid interactions
* tools for detecting molecular clusters on mobilephone surfaces

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Extra resources for Flourescence Spectroscopy

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J. K. Ilich, A. Ringler, S. S. Sedarous, D. J. Tort, and T. P. Burghardt, Biochemistry 31, 12431 (1992). 61 B. D. Hamman, A. V. Oleinikov, G. G. Jokhadze, D. E. Bochkariov, R. R. Traut, and D. M. Jameson, J. Biol. Chem. 271, 7568 (1996). [2] DESIGN OF PROFLUORESCENT PROTEASE SUBSTRATES 21 +U Excited State - - i-u G r o u n d State Monomer Dimer F]G. 2. Exciton theory. phores is perpendicular to their transition dipoles. Although previous depictions of rhodamine dimers have indicated face-to-face s t r u c t u r e s , 62-64 m o r e recent data point toward an edge-to-edge alignment between the two dyes.

The fluorophore is polar and to a first approximation it can be described as having a dipole moment in the excited state larger than that of the ground state. If the medium is apolar, the red shift in the absorption owing to the lowering of So is evidently smaller than the shift in the emission so that the stabilization of the excited state is larger than that of the ground state. The reason for this difference is found in the excess induction produced by the increased separation of charges in the excited state, acting on a solvent made up of molecules without a permanent distribution of charges.

E. Perlmann and L. Lorand, eds. Methods Enzymol. 19, (1970). 8 L. Lorand, ed. Methods Enzymol. 45, (1976). 9 L. Lorand, ed. Methods Enzymol. 80, (1981). METHODS IN ENZYMOLOGY, VOL. 278 Copyright © 1997 by Academic Press All rights of reproduction in any form reserved. 0076-6879/97 $25 16 FLUORESCENCE SPECTROSCOPY [2] proteolytic activities has received the attention of a multitude of investigators. Moreover, current interest in protease inhibitors as therapeutic agents for the treatment of metastatic cancer, inflammation, and acquired immunodeficiency syndrome (AIDS) underscores the importance of having sensitive and selective assays.

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