Laser Raman light-scattering observations of conformational changes in myosin induced by inorganic salts

Biophysical Journal
T W BarrettR M Robson

Abstract

The Raman spectra of aqueous solutions of myosin and mixtures of myosin in solutions of the salts CaCl(2), MgCl(2), and LiBr have been taken. The spectrum of the solvent background has been subtracted by means of a computer, leaving only the Raman peaks of the protein. From an analysis of the Raman bands in the regions at 900, 940, 1,240-1,300, and 1,650-1,670 cm(-1), it seems likely that CaCl(2) effects an alpha-to beta-transition in myosin, probably owing to the interaction of the Ca(2+) ion, LiBr appears to denature the protein leading to increased random coil structure, and MgCl(2) appears to have an effect intermediate between the two other salts. These results are reported for concentrations as low as 10(-5) M of CaCl(2) and MgCl(2).This investigation indicates the usefulness of the Raman light-scattering technique for the study of protein conformational changes.

Citations

Sep 16, 2011·Journal of Agricultural and Food Chemistry·Weizheng SunJiaoyan Ren
Jun 24, 2008·Critical Reviews in Food Science and Nutrition·Ana M Herrero
May 25, 1982·Biochemistry·J E Morel, M Garrigos
Mar 19, 2021·Applied Spectroscopy·Petter Vejle AndersenNils Kristian Afseth
Jul 23, 2008·Journal of Agricultural and Food Chemistry·A M HerreroF Jiménez-Colmenero
Oct 30, 2019·ACS Chemical Neuroscience·George DevittSumeet Mahajan
Jan 15, 2015·Analytical Chemistry·Rekha GautamSiva Umapathy
Dec 20, 1999·Journal of Agricultural and Food Chemistry·M OgawaS Nakai
Mar 16, 2006·Journal of Agricultural and Food Chemistry·Supawan ThawornchinsombutEunice C Y Li-Chan

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