Abstract:
:The molecular dissociation constant, Kd, is a well-established parameter to quantitate the affinity of protein-protein or other molecular interactions. Recently, we reported the theoretical basis and experimental procedure for Kd determination using a quantitative FRET method. Here we report a new development of Kd determination by measuring the reduction in donor fluorescence due to acceptor quenching in FRET. A new method of Kd determination was developed from the quantitative measurement of donor fluorescence quenching. The estimated Kd values of SUMO1-Ubc9 interaction based on this method are in good agreement with those determined by other technologies, including FRET acceptor emission. Thus, the acceptor-quenched approach can be used as a complement to the previously developed acceptor excitation method. The new methodology has more general applications regardless whether the acceptor is an excitable fluorophore or a quencher. Thus, these developments provide a complete methodology for protein or other molecule interaction affinity determinations in solution.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Jiang L,Xiong Z,Song Y,Lu Y,Chen Y,Schultz JS,Li J,Liao Jdoi
10.1038/s41598-018-35535-9subject
Has Abstractpub_date
2019-02-14 00:00:00pages
2050issue
1issn
2045-2322pii
10.1038/s41598-018-35535-9journal_volume
9pub_type
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