On the quantitative treatment of donor-donor energy migration in regularly aggregated proteins
2005 (English)In: Journal of Fluorescence, ISSN 1053-0509, E-ISSN 1573-4994, Vol. 15, no 5, 797-803 p.Article in journal (Refereed) Published
An algorithm is presented that quantitatively accounts for donor–donor energy migration (DDEM) among fluorophore-labeled proteins forming regular aggregates. The DDEM algorithm is based on Monte Carlo and Brownian dynamics simulations and applies to calculation of fluorescence depolarisation data, such as the fluorescence anisotropy. Thereby local orientations, as well as reorienting motions of the fluorescent group are considered in the absence and presence of DDEM and among, in principle, infinitely many proteins as they form regular aggregates. Here we apply the algorithm for calculating and illustrating the DDEM and the time-resolved fluorescence anisotropy under static as well as dynamic conditions within helical, linear and circular aggregate structures. A principal approach of the DDEM algorithm for analysing protein aggregates is also outlined.
Place, publisher, year, edition, pages
New York: Plenum Press , 2005. Vol. 15, no 5, 797-803 p.
Protein aggregates, protein polymers, fluorescence anisotropy, donor-donor energy migration, homo transfer, amyloid diseases, Monte Carlo simulation, Brownian dynamics
IdentifiersURN: urn:nbn:se:umu:diva-5671DOI: 10.1007/s10895-005-2989-1OAI: oai:DiVA.org:umu-5671DiVA: diva2:145265