β-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

Pietro Gervasoni; Werner Staudenmann; Peter James

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β-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

机译：β-内酰胺酶以高保护度免受氢/氘交换的构象与GroEL结合

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Escherichia coli RTEM β-lactamase revers- ibly forms a stable complex with GroEL, devoid of any enzymatic activity, at 48 deg C. When β-lactamase is diluted from this complex into denaturant solution, its unfolding rate is identical to that from the native state, while the unfolding rate from the molten globule state is too fast to be measured.

机译：大肠杆菌RTEMβ-内酰胺酶在48℃可逆地与GroEL形成稳定的复合物，没有任何酶促活性。当将β-内酰胺酶从该复合物稀释成变性溶液时，其展开速度与天然酶相同状态，而熔融小球状态的展开速度太快而无法测量。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1996年第22期|p.12189-12194|共6页
作者
Pietro Gervasoni; Werner Staudenmann; Peter James;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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6. beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange. [O] . P Gervasoni, W Staudenmann, P James, 1996

机译：β-内酰胺酶与GroEL结合的构型具有高度保护性可防止氢/氘交换。
7. beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange. [O] . Gervasoni, P, Staudenmann, W, James, P, 1996

机译：β-内酰胺酶与GroEL结合的构型具有高度保护性，可防止氢/氘交换。

β-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

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