By Joseph R. Lakowicz
This 3rd quantity information the purposes of fluorescence spectroscopy in biochemistry and biophysics.
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Additional resources for Topics in Fluorescence Spectroscopy: Biochemical Applications
The low-salt transition is pH-dependent; the anisotropy showed a pH dependence that appeared to correlate with a conformational change with a near 7. The low-salt transition also involves cation binding, with divalent cations being more than an order of magnitude more effective than monovalent cations. The low-salt transition was interpreted in terms of a two-step mechanism involving interactions between dimers of H2a and H2b with a tetramer of H3 and H4. (87) Based on the salt dependence of the decay data, the tyrosines were divided into two classes.
91) Libertini and Small(94) have identified three emissions from this residue when in the unfolded state with peaks near 300, 340, and 400 nm. The 340-nm peak was ascribed to tyrosinate (vide infra), and several possibilities were considered for the 400-nm component, including room temperature phosphorescence, emission of a charge transfer complex, or dityrosine. Dityrosine has the appropriate spectral characteristics,(96) but would require 24 J. B. Alexander Ross et al. formation of a covalent H1 dimer.
Although Tyr-138 was also perturbed by the binding of the fourth calcium, both residues appeared to be associated with high-affinity domains (III and IV). ,(116,117) using to characterize the order of binding, came to the opposite conclusion: the two high-affinity calcium sites of calmodulin are domains I and II, with subsequent filling of domain III and then domain IV. Their results seem ambiguous, however, since the calcium and terbium data differed. Whereas the first two calciums bound resulted in a substantial increase in tyrosine fluorescence and the second two calciums had only a small effect, the first two ions of bound resulted in a small enhancement of tyrosine fluorescence.