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Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence
Abstract : Femtosecond-resolved fluorescence of bacterial thymidilate synthase using a Kerr-gate based setup identifies a close-by tyrosine involved in flavin fluorescence quenching, shows that the substrate dUMP acts as a strong quencher itself and highlights functional configurational flexibility. © Owned by the authors, published by EDP Sciences, 2013
https://hal-polytechnique.archives-ouvertes.fr/hal-00943019
Contributor : Denis Roura Connect in order to contact the contributor
Submitted on : Thursday, February 6, 2014 - 8:53:09 PM
Last modification on : Tuesday, October 19, 2021 - 5:12:18 PM
Long-term archiving on: : Wednesday, May 7, 2014 - 4:40:17 AM
Contributor : Denis Roura Connect in order to contact the contributor
Submitted on : Thursday, February 6, 2014 - 8:53:09 PM
Last modification on : Tuesday, October 19, 2021 - 5:12:18 PM
Long-term archiving on: : Wednesday, May 7, 2014 - 4:40:17 AM
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epjconf_up2012_07011.pdf
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