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 |
|
|