Protein flexibility as revealed by fluorescence resonance energy transfer: an extension of the method for systems with multiple labels.
The temperature profile of the normalized fluorescence resonance energy transfer efficiency is capable of monitoring the relative change of flexibility and/or conformational state of macromolecules [Biochemistry 23 (1984) 3403]. The method described earlier for one donor-one acceptor systems is extended to multiple fluorophore systems when the energy transfer occurs between either one donor-m acceptors, or n donors-one acceptor or n donors-m acceptors (where n and m are integer values). It is shown that the normalized energy transfer efficiency obtained for systems containing multiple labels is a linear combination of the normalized transfer efficiency assigned to individual donor-acceptor pairs of the system, thus its temperature profile is capable of monitoring the change of intramolecular flexibility and/or conformational state.
Somogyi
B
B
Research Group of the Hungarian Academy of Sciences at the University of Pécs, Faculty of Medicine.
Lakos
Z
Z
Szarka
A
A
Nyitrai
M
M
D004735:Energy Transfer; D005453:Fluorescence; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods
D011506:Proteins