1 May 1998 Recent advances in protein room-temperature phosphorescence spectroscopy
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Proceedings Volume 3256, Advances in Optical Biophysics; (1998) https://doi.org/10.1117/12.307065
Event: BiOS '98 International Biomedical Optics Symposium, 1998, San Jose, CA, United States
Abstract
The use of tryptophan phosphorescence measurements in probing the structural flexibility of globular proteins in solution at room temperature has been limited to date by a number of factors which include: identification of the emitting residues, the low occurrence of tryptophan side chains in sufficiently rigid domains in globular proteins, as well as the absence of a molecular basis for the empirical correlation between phosphorescence lifetimes that are observed at room temperature, and the local viscosity. A review is presented here of our recent work in which we have attempted to address these concerns. A model for the relation between the long- lived triplet lifetimes from buried tryptophan residues and protein flexibility is described along with experimental evidence consistent with the model. Employing site-directed mutagenesis with E.coli alkaline phosphatase, we have both identified the residue responsible for the long-lived emission with the wild-type protein, as well as to reintroduce the indole side chain into alternate relatively inflexible domains resulting in the appearance of RTP.
© (1998) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Li Sun, Li Sun, Evan R. Kantrowitz, Evan R. Kantrowitz, William C. Galley, William C. Galley, } "Recent advances in protein room-temperature phosphorescence spectroscopy", Proc. SPIE 3256, Advances in Optical Biophysics, (1 May 1998); doi: 10.1117/12.307065; https://doi.org/10.1117/12.307065
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