concanavalin-a and 10-camphorsulfonic-acid

A synchrotron-radiation-based circular-dichroism end-station has been implemented at beamline BL04B at the National Synchrotron Radiation Research Center (NSRRC) in Taiwan for biological research. The design and performance of this compact end-station for measuring circular-dichroism spectra in the vacuum-ultraviolet region are described. The linearly polarized light from the beamline is converted to modulated circularly polarized light with a LiF photoelastic modulator to provide a usable wavelength region of 130-330 nm. The light spot at the sample position is 5 mm × 5 mm at a slit width of 300 µm and provides a flux greater than 1 × 10(11) photons s(-1) (0.1% bandwidth)(-1). A vacuum-compatible cell made of two CaF(2) windows has a variable path length from 1.3 µm to 1 mm and a temperature range of 253-363 K. Measured CD spectra of (1S)-(+)-10-camphorsulfonic acid and proteins demonstrated the ability of this system to extend the wavelength down to 172 nm in aqueous solution and 153 nm in hexafluoro-2-propanol.

Topics: Camphor; Circular Dichroism; Concanavalin A; Myoglobin; Protein Folding; Protein Structure, Secondary; Proteins; Serum Albumin, Bovine; Solutions; Synchrotrons