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Science 30 May 1975:
Vol. 188. no. 4191, pp. 933 - 936
DOI: 10.1126/science.1138362
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Articles

Science, Vol 188, Issue 4191, 933-936
Copyright © 1975 by American Association for the Advancement of Science

articles

Laser raman spectroscopy--new probe of myosin substructure

EB Carew, IM Asher, and HE Stanley

Laser Raman spectroscopy is used to probe the heterogeneous substructure of the large contractile protein myosin. Some peaks are assigned to specific chemical groups of the molecule; others, notably the conformationally sensitive amide III vibrations, provide information on the structurally distinct regions of the molecule. Deuteration of the NH groups is instrumental in the assignment of these vibrational modes. The relative intensities of bands typical of alpha-helical conformations (near 1265 and 1304 cm-1) and bands associated with nonhelical structure (near 1244 cm-1) are sensitive indicators of myosin substructure and represent potentially useful probes of conformational changes.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Opsin structure probed by raman spectroscopy of photoreceptor membranes.
K. Rothschild, Andrew JR, W. De Grip, and H. Stanley (1976)
Science 191, 1176-1178
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Electrostatic and Steric Effects in the Selective Complexation of Cations in Nonactin.
G. D. J. Phillies, I. M. Asher, and H. E. Stanley (1975)
Science 188, 1027-1029
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