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Alpha-Helical Structure of Fish Actomyosin: Changes during Setting
Authors:MASAHIRO OGAWA  JUN KANAMARU  HIROKI MIYASHITA  TORU TAMIYA  TAKAHIDE TSUCHIYA
Affiliation:The authors are with the Dept. of Chemistry, Faculty of Science &Technology, Sophia Univ., 7–1 Kioi-cho, Chiyoda-ku, Tokyo 102, Japan.
Abstract:
Participation of the α-helix in setting was investigated using circular dichroism. The α-helicity of the actomyosin from eight species of fish decreased during incubation at 30°C or at 40°C. The extent and pattern of decrease differed among species. When rate of decrease was plotted vs rate of increase in strength of gel preincubated at 30°C or at 40°C, the two factors correlated closely. We propose that the unfolding of α-helix initiated setting.
Keywords:fish    actomyosin    circular dichroism    alpha helix
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