Predictability of weak binding from X-ray crystallography: inhaled anesthetics and myoglobin.
Predictability of weak binding from X-ray crystallography: inhaled anesthetics and myoglobin.
复制标题
X 射线晶体学弱结合的可预测性：吸入麻醉剂和肌红蛋白。
DOI：
10.1021/bi001428d
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发表时间：
2001
期刊：
影响因子：
2.9
通讯作者：
Eckenhoff,RG
中科院分区：
文献类型：
--
作者：
Tanner,JW;Johansson,JS;Liebman,PA;Eckenhoff,RG
氙和二氯甲烷是吸入麻醉剂，其与肌红蛋白的结合已通过X射线晶体学证明。我们探索这种结合的热力学意义，使用差示扫描量热法，圆二色光谱，和氢-氚交换测量研究这些代理肌红蛋白折叠稳定性的影响。虽然这些麻醉剂的特异性结合可能会稳定肌红蛋白对展开，二氯甲烷实际上不稳定肌红蛋白在所有检查浓度的麻醉剂（15，40和200 mM）。另一方面，氙（1大气压）稳定肌红蛋白。因此，二氯甲烷和氙对肌红蛋白的稳定性有相反的影响，尽管定位在折叠的X射线晶体结构中。这些结果表明，如果要了解弱结合蛋白质的后果，需要溶液测量来补充晶体学。
Xenon and dichloromethane are inhalational anesthetic agents whose binding to myoglobin has been demonstrated by X-ray crystallography. We explore the thermodynamic significance of such binding using differential scanning calorimetry, circular dichroism spectroscopy, and hydrogen−tritium exchange measurements to study the effect of these agents on myoglobin folding stability. Though specific binding of these anesthetics might be expected to stabilize myoglobin against unfolding, dichloromethane actually destabilized myoglobin at all examined concentrations of this anesthetic (15, 40, and 200 mM). On the other hand, xenon (1 atm) stabilized myoglobin. Thus, dichloromethane and xenon have opposite effects on myoglobin stability despite localization in comparably folded X-ray crystallographic structures. These results suggest a need for solution measurements to complement crystallography if the consequences of weak binding to proteins are to be appreciated.