A search for protein structural changes accompanying the contractile interaction.
A search for protein structural changes accompanying the contractile interaction.
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寻找伴随收缩相互作用的蛋白质结构变化。
DOI：
10.1073/pnas.88.21.9748
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发表时间：
1991
影响因子：
11.1
通讯作者：
Morales,MF
中科院分区：
文献类型：
--
作者：
JohnsonJr,WC;Bivin,DB;Ue,K;Morales,MF
似乎肌球蛋白S-1颗粒区域的微小运动（迄今为止仅通过荧光共振能量转移测量和交联研究检测到）可能介导收缩系统中的化学机械能量转导。在这里，我们发现在10摄氏度和20摄氏度的高精度条件下，ATP与S-1结合会导致CD信号（δ epsilon 222）的微小（0.4%）变化，就像16摄氏度以下的温度变化一样。ATP结合会干扰我们现在认为位于可移动区域的色氨酸残基，我们发现温度影响色氨酸荧光的方式与影响CD信号的方式大致相同。因此，我们认为CD信号报告了S-1中与转导相关的运动。如果S-1暴露在16-30℃范围内，CD信号随温度下降；ATP抵消了这个下降。真空紫外CD光谱分析得到42%的α -螺旋结构、9%的反平行β -片结构、7%的平行β -片结构、14%的β -匝结构和29%的其他结构。
It appears that small movements (detected hitherto only by fluorescence resonance energy transfer measurements and crosslinking studies) in a region of the myosin S-1 particle may mediate chemomechanical energy transduction in the contractile system. Here we find under conditions of high precision at 10 degrees C and 20 degrees C that ATP binding to S-1 causes small (0.4%) changes in CD signal, delta epsilon 222, as do temperature changes in the regime below 16 degrees C. ATP binding perturbs tryptophan residues that we now think are in the mobile region, and we find here that temperature affects tryptophan fluorescence in much the same way that it affects the CD signal, so we believe that the CD signal reports transduction-related movements in S-1. If S-1 is exposed to the range 16-30 degrees C, CD signal falls with temperature; ATP counteracts this fall. Analysis of vacuum-UV CD spectra yields 42% alpha-helix, 9% antiparallel beta-sheet, 7% parallel beta-sheet, 14% beta-turns, and 29% other structures.