Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure

Carey D. Waldburger; Thorlakur Jonsson; Robert T. Sauer

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Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure

机译：蛋白质折叠的障碍：掩埋极性相互作用的形成是获得结构的缓慢步骤

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In the MYL mutant of the Arc repressor dimer, sets of partially buried salt-bridge and hydrogen-bond interactions mediated by Arg-31, Glu-36, and Arg-40 in each subunit are replaced by hydrophobic interactions between Met-31, Tyr-36, and Leu-40. The MYL refolding/dimerization reaction differs from that of wild type in being 10- to 1250-fold faster, having an earlier transition state, and depending upon viscosity but not ionic strength.

机译：在Arc阻遏物二聚体的MYL突变体中，每个亚基中由Arg-31，Glu-36和Arg-40介导的部分掩埋的盐桥和氢键相互作用集被Met-31，Tyr之间的疏水相互作用取代-36和Leu-40。 MYL重折叠/二聚反应与野生型的不同之处在于其快10至1250倍，具有较早的过渡态，并且取决于粘度而不是离子强度。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1996年第7期|p.2629-2634|共6页
作者
Carey D. Waldburger; Thorlakur Jonsson; Robert T. Sauer;
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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. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. [O] . C D Waldburger, T Jonsson, R T Sauer 1996

机译：蛋白质折叠的障碍：掩埋极性相互作用的形成是获得结构的缓慢步骤。
7. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. [O] . Waldburger, C D, Jonsson, T, Sauer, R T 1996

机译：蛋白质折叠的障碍：掩埋极性相互作用的形成是获得结构的缓慢步骤。

Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure

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