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Tracing the conformational changes in BSA using FRET with environmentally-sensitive squaraine probes
Autor:
Leonid D. Patsenker, Anatoliy L. Tatarets, Ewald A. Terpetschnig, Gary Gellerman, Iryna V Govor, Olena M. Obukhova
Publikováno v:
Methods and applications in fluorescence. 4(2)
A new potential method of detecting the conformational changes in hydrophobic proteins such as bovine serum albumin (BSA) is introduced. The method is based on the change in the Forster resonance energy transfer (FRET) efficiency between protein-sens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79cba884edc8a68f64aeaca75708c881
https://pubmed.ncbi.nlm.nih.gov/28809172
https://pubmed.ncbi.nlm.nih.gov/28809172
