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Abstract : In the histidine kinase family, the HAMP and DHp domains are considered to play an important role into the transmission of signal arising from environmental conditions to the auto-phosphorylation site and to the binding site of response regulator. Several conformational motions inside HAMP have been proposed to transmit this signal: (i) the gearbox model, (ii) α helices rotations, pistons and scissoring, (iii) transition between ordered and disordered states. In the present work, we explore by temperature-accelerated molecular dynamics (TAMD), an enhanced sampling technique, the conformational space of the cytoplasmic region of histidine kinase CpxA. Several HAMP motions, corresponding to α helices rotations , pistoning and scissoring have been detected and correlated to the segmental motions of HAMP and DHp domains of CpxA.
https://hal-pasteur.archives-ouvertes.fr/pasteur-02330083 Contributor : Therese MalliavinConnect in order to contact the contributor Submitted on : Wednesday, October 23, 2019 - 6:11:21 PM Last modification on : Thursday, April 7, 2022 - 10:10:37 AM Long-term archiving on: : Friday, January 24, 2020 - 9:06:21 PM