Raman spectroscopy of cytoplasmic muscle fiber proteins. Orientational order.
The polarized Raman spectra of glycerinated and intact single muscle fibers of the giant barnacle were obtained. These spectra show that the conformation-sensitive amide I, amide III, and C-C stretching vibrations give Raman bands that are stronger when the electric field of both the incident and scattered radiation is parallel to the fiber axis (Izz). The detailed analysis of the amide I band by curve fitting shows that approximately 50% of the alpha-helical segments of the contractile proteins are oriented along the fiber axis, which is in good agreement with the conformation and composition of muscle fiber proteins. Difference Raman spectroscopy was also used to highlight the Raman bands attributed to the oriented segments of the alpha-helical proteins. The difference spectrum, which is very similar to the spectrum of tropomyosin, displays amide I and amide III bands at 1,645 and 1,310 cm-1, respectively, the bandwidth of the amide I line being characteristic of a highly alpha-helical biopolymer with a small dispersion of dihedral angles. A small dichroic effect was also observed for the band due to the CH2 bending mode at 1,450 cm-1 and on the 1,340 cm-1 band. In the C-C stretching mode region, two bands were detected at 902 and 938 cm-1 and are both assigned to the alpha-helical conformation.
Pézolet
M
M
Département de Chimie, Faculté des Sciences et de Génie, Université Laval, Sainte-Foy, Québec, Canada.
Pigeon
M
M
Ménard
D
D
Caillé
J P
JP
D000577:Amides; D000818:Animals; D008854:Microscopy, Electron; D009038:Motion; D009132:Muscles / Q000648:ultrastructure*; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman; D001468:Thoracica; D014335:Tropomyosin
D000577:Amides; D014335:Tropomyosin