Extended Förster theory for determining intraprotein distances: 1. The K2-dynamics and fluorophore reorientation
2004 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, Vol. 108, no 44, 17243-17250 p.Article in journal (Refereed) Published
A detailed analysis of the previously developed (J. Chem. Phys. 1996, 105, 10896) extended Förster theory (EFT) is presented for analyzing electronic energy migration within pairs of donors (D). Synthetic data that mimics experimental time-correlated single photon counting data were generated and re-analyzed. To cover a wide dynamic range and various orientational restrictions, the rates of reorientation, as well as the orientational configurations of the interacting D-groups were varied. In general DD distances are recovered within an error limit of 5%, while the errors in orientational configurations are usually larger. The Maier−Saupe and cone potentials were used to generate an immense variety of orientational trajectories. The results obtained exhibit no significant dependence on the choice of potential function used for generating EFT data. Present work demonstrates how to overcome the classical “κ2-problem” and the frequently applied approximation of κ2 = 2/3 in the data analyses. This study also outlines the procedure for analyzing fluorescence depolarization data obtained for proteins, which are specifically labeled with D-groups. The EFT presented here brings the analyses of DDEM data to the same level of molecular detail as in ESR- and NMR-spectroscopy.
Place, publisher, year, edition, pages
2004. Vol. 108, no 44, 17243-17250 p.
Thimerosal, Ethylmercury, Mice, Autoimmunity
IdentifiersURN: urn:nbn:se:umu:diva-2134DOI: 10.1021/jp040423dOAI: oai:DiVA.org:umu-2134DiVA: diva2:139964