Differential scanning calorimetry of a conformational transition in heavy meromyosin.
Differential scanning calorimetry of a conformational transition in heavy meromyosin.
复制标题
重粒肌球蛋白构象转变的差示扫描量热法。
DOI：
10.1016/0003-9861(90)90669-p
复制
发表时间：
1990
影响因子：
3.9
通讯作者：
Shriver,JW
中科院分区：
文献类型：
--
作者：
Shriver,JW
我们研究了差示扫描量热法 (DSC) 表征蛋白质构象变化的潜在用途，重点关注肌球蛋白头部的构象变化，这可能与在肌肉收缩时提供力量的动力冲程有关。模拟表明，热函变化大于约 30 kcal/mol 的两态构象转变应该可以通过 DSC 观察到。我们在此介绍重粒肌球蛋白预变性结构变化的差示扫描量热研究。这些实验所需的高浓度蛋白质导致分子间相互作用的潜在贡献。讨论了通过 DSC 研究构象转变相关的技术困难。
We have investigated the potential use of differential scanning calorimetry (DSC) to characterize conformational changes in proteins with emphasis on a conformational change in the myosin head which may be related to the power-stroke providing force production in muscle contraction. Simulations indicate that two-state conformational transitions with enthalpy changes greater than approximately 30 kcal/mol should be observable by DSC. We present here differential scanning calorimetric studies of a predenaturation structural change in heavy meromyosin. The high concentration of protein required for these experiments leads to potential contributions from intermolecular interactions. The technical difficulties associated with studying conformational transitions by DSC are discussed.