Abstract

Fluorescence resonance energy transfer spectroscopy (FRET) has been widely used to determine distances ranging from 10 to 100 A between amino acids within proteins. However, FRET is not very good at measuring atomic distances because it measures the distance between two probes attached to an amino acid but not the position of the amino acid itself. Therefore, one has to take into consideration the size of the probes used to interpret the FRET data. FRET compensates for that deficit by being particularly sensitive to changes in distance and therefore is suitable to study conformational change in proteins (dos Remedios and Moens 1995a, 1995b).

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