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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >THERMAL UNFOLDING OF ACANTHAMOEBA MYOSIN 11 AND SKELETAL MUSCLE MYOSIN
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THERMAL UNFOLDING OF ACANTHAMOEBA MYOSIN 11 AND SKELETAL MUSCLE MYOSIN

机译：棘阿米巴肌球蛋白11和骨骼肌肌球蛋白的热解折叠

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摘要

Studies on the thermal unfolding of monomeric Acanthamoeba myosin II and other myosins, in particular skeletal muscle myosin, using differential scanning calorimetry (DSC) are reviewed. The unfolding transitions for intact myosin or its head fragment are irreversible, whereas those of the rod part and its fragments are completely reversible, Acanthamoeba myosin II unfolds with a high degree of cooperativity from ca, 40-45 degrees C at pH 7.5 in 0.6 M KCl, producing a single, sharp endotherm in DSC. In contrast, thermal transitions of rabbit skeletal muscle myosin occur over a broader temperature range (ca, 40-60 degrees C) under the same conditions, The DSC studies on the unfolding of the myosin rod and its fragments allow identification of cooperative domains, each of which unfolds according to a two-state mechanism, Also, DSC data show the effect of the nucleotide-induced conformational changes in the myosin head on the protein stability. [References: 45]
机译：审查了使用差示扫描量热法（DSC）研究单体棘阿米巴肌球蛋白II和其他肌球蛋白，特别是骨骼肌肌球蛋白的热展开。完整的肌球蛋白或其头部片段的展开转变是不可逆的，而杆状部分及其片段的展开转变是完全可逆的，Acanthamoeba myosin II可以在40-45摄氏度，pH 7.5、0.6 M的条件下以高协同性展开KCl，在DSC中产生单一的尖峰吸热。相反，在相同条件下，兔骨骼肌肌球蛋白的热转变发生在更宽的温度范围内（约40-60摄氏度）。DSC对肌球蛋白棒及其片段的展开的研究允许鉴定协作域，每个DSC数据还显示了肌球蛋白头部中核苷酸诱导的构象变化对蛋白质稳定性的影响。 [参考：45]

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