Abstract
So far our view of protein function is formed, to a significant extent, by traditional structure determination showing many beautiful static protein structures. Recent experiments by single-molecule and other techniques have questioned the idea that proteins and other biomolecules are static structures. We used multi-parameter fluorescence detection (MFD) to perform smFRET studies of free diffusing biomolecules. We demonstrate that the simultaneous acquisition of most fluorescent parameters by MFD allows for a robust assessment of all possible artefacts involved in single-molecules FRET and offers unsurpassed capabilities regarding the identification and analysis of individual species present in population of molecules [1].
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