Effect of Diffusion on Resonance Energy Transfer Rate Distributions: Implications for Distance Measurements.

ABSTRACT: Intrinsically disordered protein regions and many other biopolymers lack the three-dimensional structure that could be determined by X-ray crystallography or NMR, which encourages the application of alternative experimental methods. Time-resolved resonance energy transfer data are often used to measure distances between two fluorophores attached to a flexible biopolymer. This is complicated by the rotational and translational diffusion of the fluorophores and by nonmonoexponential donor decay in the absence of the acceptor. Equation I(DA)(t) = I(D)(t)·F(t) is derived here, which is applicable regardless of whether I(D)(t) is monoexponential. I(D)(t) and I(DA)(t) are the δ-excitation donor emission decays in the absence and in the presence of the acceptor; F(t) contains information about en

SUBMITTER: Toptygin D 

PROVIDER: S-EPMC8785435 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature