Abstract
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.
Original language | English |
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Pages (from-to) | 78-85 |
Number of pages | 8 |
Journal | Applied spectroscopy |
Volume | 50 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1996 |
Keywords
- Polarization-sensitive CARS
- Multichannel raman
- Conformation of proteins