Cdf 426s l peltier system

Far-UV circular dichroism (CD) data was acquired using a Jasco Model J-810 spectropolarimeter connected to a CDF-426S/L Peltier system (Jasco). Purified protein samples were prepared at 0.1 mg/ml in 5 mM phosphate buffer pH 7.4 (filtered and degassed) and analysed using a 0.1 cm cuvette. 10 scans were acquired for each sample at 37 °C at a bandwidth of 1 nm, a sensitivity of 5 millidegrees, and continuous scanning mode at a speed of 100 nm/min. Data was plotted as the mean values for all scans. Far-UV (190–250 nm) CD spectra was recorded and analysed using DichroWeb software against the SMP 180 data set optimised for 190–240 nm using the CONTIN program^{35 (link),36 (link)}. For FT-IR spectroscopy, 20 μl of purified rCLU or pCLU (at 10 μM in PBS) was added into a BioATR cell. Samples were acquired in absorbance mode at 37 °C on a Vertex 70 FT-IR spectrometer (Bruker Optics, UK) and corrected for the absorption spectra of PBS.

A Jasco Model J-810 (Jasco, Easton, MD, USA) spectropolarimeter linked to a CDF-426S/L Peltier system (Jasco) was used to acquire circular dichroism (CD) data. Far-UV (180–250 nm) CD studies were undertaken to compare the secondary structure of proteins. Samples were analysed using a 1 mm CD cell, acquiring spectra at a sensitivity of 100 millidegrees and a bandwidth of 1 nm. The scanning mode was continuous at 50 nm/min and 6 data sets were accumulated before the average was displayed.