Nuclear inelastic scattering studies of a 1D- polynuclear spin crossover complex of Fe(II) urea-triazoles

The partial density of vibrational states (pDOS) of the low-spin isomer of the tosylate salt of [Fe{(N-Propyl)-N′-(1,2,4-triazole-4-yl-urea)}$_3$]$^{2+}$ was determined by nuclear inelastic scattering experiments performed at 8 K. The pDOS features a rich band structure from 320 to 500 cm$^{−1}$, characteristic of the low spin state of the complex. Density functional theory calculations (B3LYP/CEP-31G) were used to assign molecular modes to the experimentally observed peak in the pDOS

Interdependence of TbKIN-C and TbKIN-D for their stability in the procyclic form.

<p>(<b>A</b>). Western blot to detect TbKIN-D protein level in TbKIN-C RNAi cells and TbKIN-C protein level in TbKIN-D RNAi cells in the procyclic form. MG132 (50 µM) was added to TbKIN-C RNAi cells and TbKIN-D RNAi cells at day 2 of RNAi induction and incubated for 8 hrs. (<b>B</b>). TbKIN-C and TbKIN-D mRNA level in TbKIN-C RNAi cells and TbKIN-D RNAi cells measured by quantitative RT-PCR in the procyclic form. (<b>C</b>). Stability of TbKIN-C and TbKIN-D proteins in wild-type procyclic cells. Cells were treated with cycloheximide and time-course samples were immunoblotted with anti-HA antibody to detect the levels of TbKIN-C-3HA and TbKIN-D-3HA proteins. TbAUK1, the Aurora-like kinase in trypanosomes that is known to be degraded by the proteasome, was included as the positive control. Levels of TbPSA6 protein was monitored to serve as the loading control.</p