Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1992 Oct;63(4):976–985. doi: 10.1016/S0006-3495(92)81691-0

Polarization sensitive coherent anti-Stokes Raman scattering spectroscopy of the amide I band of proteins in solutions.

A Y Chikishev 1, G W Lucassen 1, N I Koroteev 1, C Otto 1, J Greve 1
PMCID: PMC1262235  PMID: 1330043

Abstract

Polarization sensitive coherent anti-Stokes Raman scattering (PCARS) spectroscopy is a fruitful technique to study Raman vibrations of diluted molecules under off-electron resonant conditions. We apply PCARS as a direct spectroscopic method to investigate the broad amide I band of proteins in heavy water. In spontaneous Raman spectroscopy, this band is not well resolved. We fit a number of spectra taken of each protein under different polarization conditions, with a single set of parameters. It then appears that some substructure is observed in the amide I band. From this substructure, we determine the percentage of alpha-helix, beta-sheet, and random coil for the proteins lysozyme, albumin, ribonuclease A, and alpha-chymotrypsin.

Full text

PDF
976

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barela T. D., Darnall D. W. Practical aspects of calculating protein secondary structure from circular dichroism spectra. Biochemistry. 1974 Apr 9;13(8):1694–1700. doi: 10.1021/bi00705a022. [DOI] [PubMed] [Google Scholar]
  2. Byler D. M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 1986 Mar;25(3):469–487. doi: 10.1002/bip.360250307. [DOI] [PubMed] [Google Scholar]
  3. Chang C. T., Wu C. S., Yang J. T. Circular dichroic analysis of protein conformation: inclusion of the beta-turns. Anal Biochem. 1978 Nov;91(1):13–31. doi: 10.1016/0003-2697(78)90812-6. [DOI] [PubMed] [Google Scholar]
  4. Greenfield N., Fasman G. D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 1969 Oct;8(10):4108–4116. doi: 10.1021/bi00838a031. [DOI] [PubMed] [Google Scholar]
  5. KRIMM S. Infrared spectra and chain conformation of proteins. J Mol Biol. 1962 Jun;4:528–540. doi: 10.1016/s0022-2836(62)80107-7. [DOI] [PubMed] [Google Scholar]
  6. Levitt M., Greer J. Automatic identification of secondary structure in globular proteins. J Mol Biol. 1977 Aug 5;114(2):181–239. doi: 10.1016/0022-2836(77)90207-8. [DOI] [PubMed] [Google Scholar]
  7. Lippert J. L., Tyminski D., Desmeules P. J. Determination of the secondary structure of proteins by laser Raman spectroscopy. J Am Chem Soc. 1976 Oct 27;98(22):7075–7080. doi: 10.1021/ja00438a057. [DOI] [PubMed] [Google Scholar]
  8. Lord R. C., Yu N. T. Laser-excited Raman spectroscopy of biomolecules. II. Native ribonuclease and alpha-chymotrypsin. J Mol Biol. 1970 Jul 28;51(2):203–213. doi: 10.1016/0022-2836(70)90137-3. [DOI] [PubMed] [Google Scholar]
  9. Marx J., Jacquot J., Berjot M., Puchelle E., Alix A. J. Characterization and conformational analysis by Raman spectroscopy of human airway lysozyme. Biochim Biophys Acta. 1986 Apr 22;870(3):488–494. doi: 10.1016/0167-4838(86)90257-8. [DOI] [PubMed] [Google Scholar]
  10. Nestor J., Spiro T. G., Klauminzer G. Coherent anti-Stokes Raman scattering (CARS) spectra, with resonance enhancement, of cytochrome c and vitamin B12 in dilute aqueous solution. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3329–3332. doi: 10.1073/pnas.73.10.3329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Otto C., de Mul F. F., Harmsen B. J., Greve J. A Raman scattering study of the helix-destabilizing gene-5 protein with adenine-containing nucleotides. Nucleic Acids Res. 1987 Sep 25;15(18):7605–7625. doi: 10.1093/nar/15.18.7605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pézolet M., Pigeon M., Ménard D., Caillé J. P. Raman spectroscopy of cytoplasmic muscle fiber proteins. Orientational order. Biophys J. 1988 Mar;53(3):319–325. doi: 10.1016/S0006-3495(88)83109-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Williams R. W., Dunker A. K. Determination of the secondary structure of proteins from the amide I band of the laser Raman spectrum. J Mol Biol. 1981 Nov 15;152(4):783–813. doi: 10.1016/0022-2836(81)90127-3. [DOI] [PubMed] [Google Scholar]
  14. Williams R. W. Estimation of protein secondary structure from the laser Raman amide I spectrum. J Mol Biol. 1983 Jun 5;166(4):581–603. doi: 10.1016/s0022-2836(83)80285-x. [DOI] [PubMed] [Google Scholar]
  15. Yu T. J., Lippert J. L., Peticolas W. L. Laser Raman studies of conformational variations of poly-L-lysine. Biopolymers. 1973;12(9):2161–2175. doi: 10.1002/bip.1973.360120919. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES