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Secondary Structure of Bovine Albumin as Studied by Polarization-Sensitive Multiplex CARS Spectroscopy

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The first application of polarization-sensitive multiplex coherent anti-Stokes Raman spectroscopy (MCARS) in the absence of resonance enhancement to the resolution of the secondary structure of a protein in solution is reported. Polarization MCARS spectra of bovine albumin in D2O were obtained in the range 1370 to 1730 cm-1 with the aid of the background suppression technique. The spectra were fitted simultaneously with a single set of parameters (band positions, bandwidths, amplitudes, and depolarization ratios). Polarized Raman spectra simulated with these parameters revealed a good correspondence with the spontaneous Raman spectra measured. The broad amide I band was decomposed assuming the three major secondary conformations of protein, of which the contribution of β-sheet structure was found to be negligible. Relative weights of α-helix and random coil conformations agree well with the estimates obtained with Raman and circular dichroism (CD) spectroscopies.

Keywords: Conformation of proteins; Multichannel Raman; Polarization-sensitive CARS

Document Type: Research Article


Affiliations: Institute for Biomedical Technology (BMTI) and Applied Optics Group, Department of Applied Physics, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands

Publication date: January 1, 1996

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