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首页> 外文期刊>Biochemistry >Predictability of weak binding from x-ray crystallography:inhaled anesthetics and myoglobin
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Predictability of weak binding from x-ray crystallography:inhaled anesthetics and myoglobin

机译：X射线晶体学分析弱结合的可预测性：吸入麻醉药和肌红蛋白

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摘要

Xenon and dichioromethane 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, dichioromethane 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.
机译：氙气和双氯甲烷是吸入麻醉剂，其与肌红蛋白的结合已通过X射线晶体学证实。我们使用差示扫描量热法，圆二色光谱和氢-tri交换测量来研究此类结合的热力学意义，以研究这些试剂对肌红蛋白折叠稳定性的影响。尽管可以预期这些麻醉剂的特异性结合会稳定肌红蛋白的抗折叠性，但是在所有麻醉剂浓度（15、40和200 mM）下，二氯甲烷实际上都会使肌红蛋白不稳定。另一方面，氙气（1 atm）稳定了肌红蛋白。因此，尽管存在于折叠的X射线晶体结构中，但双氯甲烷和氙气对肌红蛋白的稳定性却具有相反的影响。这些结果表明，如果要认识到与蛋白质弱结合的后果，则需要进行溶液测量以补充晶体学。

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