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Differences in solution dynamics between lens beta-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation

机译:氢-氘交换和脱酰胺法检测晶状体β-晶体蛋白同二聚体和异二聚体之间溶液动力学的差异

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摘要

Background: Lens transparency is due to the ordered arrangement of the major structural proteins, called aystallins. beta B2 crystallin in the lens of the eye readily forms dimers with other beta-crystallin subunits, but the resulting heterodimer structures are not known and were investigated in this study.
机译:背景:晶状体透明性是由于被称为aystallins的主要结构蛋白的有序排列所致。眼晶状体中的βB2晶状体蛋白容易与其他β-晶状体蛋白亚基形成二聚体,但尚不知道所得的异二聚体结构,并已在本研究中进行了研究。

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