Key result
Skeletal muscle tropomyosin is flexible in the middle of the molecule, with trypsin susceptibility increasing upon lowering ionic strength or raising temperature.
Skeletal muscle tropomyosin is flexible in the middle of the molecule, contrasting with the flanking N- and C-terminal trypsin-resistant segments.
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Rabbit skeletal tropomyosin flexibility data should not change clinical practice; leaves open cardiac isoform dynamics and disease relevance.
Structural changes in tropomyosin from rabbit skeletal muscle were studied by the tryptic digestion method, which is an application of the quantitative enzyme-probe method recently developed by Ueno and Harrington [Ueno, H., & Harrington, W.F. (1984) J. Mol. Biol. 173, 35-61]. Effects of ionic strength, temperature, and an interchain disulfide bond at Cys-190 on the structure of tropomyosin were examined. A region of high susceptibility to trypsin was found to be localized in the middle portion of the molecule, and its susceptibility increased on lowering ionic strength and/or raising temperature. With the introduction of a disulfide bond at Cys-190, cleavage on the N-terminal side of Cys-190 was accelerated. The results suggest that skeletal muscle tropomyosin is flexible in the middle of the molecule in contrast to the flanking N- and C-terminal trypsin-resistant segments.
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Hitoshi Ueno (1984) studied this question. Environmental changes and disulfide bond introduction was evaluated on Structural changes and trypsin susceptibility. Skeletal muscle tropomyosin is flexible in the middle of the molecule, with trypsin susceptibility increasing upon lowering ionic strength or raising temperature.
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