By Franco Bassani (auth.), David M. Jameson, Gregory D. Reinhart (eds.)
This quantity relies on a world symposium held in the course of September 9-12, 1986 in Bocca di Magra, Italy. The cause of the organizers was once to collect professional practitioners of fluorescence spectroscopy, fairly as utilized to organic structures, to evaluate fresh advancements within the box and talk about destiny instructions. while the assembly was once meant to honor the singular and amazing medical profession of Gregorio Weber at the social gathering of his 70th birthday. Gregorio Weber is actually the pioneer within the software of fluores cence easy methods to biochemistry and biophysics. an entire checklist of his medical contributions to fluorescence and to protein biochemistry is past the scope of this preface. Suffice it to claim that seeing that his preliminary landmark articles on fluorescence, released within the past due 1940's and early 1950's, Gregorio Weber has endured to make seminal contribu tions to either the idea and perform of fluorescence and, opposite to many that may be tempted to leisure on their laurels, he exhibits no symptoms of slackening his speed. as well as his extra seen tangible contributions to the medical box, Gregorio Weber has made both beneficial contributions of one other kind. particularly, he has had the main profound influence, either profeSSionally and in my opinion, on generations of younger scientists.
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Extra resources for Fluorescent Biomolecules: Methodologies and Applications
Example text
60 0.. -J o 100 200 TIME 300 (SEC) 400 500 600 100 200 300 400 500 600 TIME (SEC) Figure 6. Kinetics of the reaction of pyrene maleimide with Enzyme I. 5 and 1 mM EDTA. 25 mg/ml and pyrene concentration was 20 ~M. Presence of 5 mM Mg2+ and Mg2+ plus PEP (2 mM) influenced the reactivity of -SH groups. B) Changes of Trp fluorescence upon reaction of pyrene to Enzyme I were monitored at 340 nm with an excitation of 295 nm. Conditions were the same as in A. Measurements were obtained with an S1M 8000 photon counting spectrofluorometer.
The two general trends of the characteristic parameters of the lifetime distribution observed as the temperature was changed can be qualitatively explained as follows. As the temperature increases, the rate at which the protein fluctuates among different conformations increases. The localized environment in the protein matrix experienced by the tryptophan residue during its excited lifetime becomes more homogeneous which leads to a more homogeneous decay, with the result that the distribution narrows.
Are obtained from the following relationships: P M = tan- 1(S/G) (6) (7) 23 METHODOLOGY The fluorescence decay was measured by use of multifrequency phase fluorometry (Gratton & Limkeman, 1983) on an instrument which utilizes the harmonic content of a mode-locked', synchronously pumped and frequency doubled dye laser as an excitation source. , 1985). 06 nm, approximately. , 1980). was assigned to this reference. 99 ns An excitation polarizer at 55 0 with respect to the horizontal was used to eliminate possible polarization effects.