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.
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Ogawa et al. (1995) studied this question.
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