Topics in Fluorescence Spectroscopy: Biochemical by Joseph R. Lakowicz

By Joseph R. Lakowicz

This 3rd quantity information the functions of fluorescence spectroscopy in biochemistry and biophysics.

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On the other hand, a static mechanism involving formation of a dark complex should exhibit only a 1/T temperature dependence for the logarithm of the equilibrium association constant. (69) concluded that the disulfide quenching interaction was primarily static in nature. From the dithiothreitol quenching of the six tyrosines in native bovine pancreatic ribonuclease, the reduced and S-methylated form of the enzyme, and N-acetyltyrosine-N'-methylamide, and using 1 M as the standard state at 298 K, the average thermodynamic parameters obtained for complex formation were From the magnitude and positive sign of it was suggested that hydrophobicity could be important in stabilizing the tyrosyl–disulfide complex.

On the surface of proteins, this process is thought to involve transient hydrogen bonds; obviously, water will compete for formation of hydrogen bonds. Under these circumstances, aspartate or glutamate side chains would have to be very close to the phenol ring to be effective. On the basis of studies of tyrosine copolymers, Longworth (1) concluded that carboxylate quenching does not proceed via excited-state proton transfer, even though it has been observed that ionization of the phenol hydroxyl group leads to a dramatic reduction in the fluorescence quantum yield.

120)confirmed the observations by Kilhoffer et al. of two high-affinity sites at domains I and II and two lowaffinity sites at domains III and IV. (121) also examined the order of filling the lanthanide binding sites and concluded that domains III and IV are indeed occupied subsequent to domains I and II. Domains I and II, however, appeared to have quite different affinities for terbium: one of these two sites was occupied first, and the other second. (122) then reexamined the relationship between calcium and terbium binding by stopped-flow kinetic studies and reported that, contrary to what was thought earlier, calcium and lanthanides in fact exhibit opposite preferences for the four metal-binding sites of calmodulin.

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