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Refolding and reactivation of Escherichia coli tryptophan synthase beta2 subunit after inactivation and dissociation in guanidine hydrochloride at acidic pH.

作者信息

Groha C, Bartholmes P, Jaenicke R

出版信息

Eur J Biochem. 1978 Dec;92(2):437-41. doi: 10.1111/j.1432-1033.1978.tb12764.x.

DOI:10.1111/j.1432-1033.1978.tb12764.x
PMID:33046
Abstract
摘要

相似文献

1
Refolding and reactivation of Escherichia coli tryptophan synthase beta2 subunit after inactivation and dissociation in guanidine hydrochloride at acidic pH.
Eur J Biochem. 1978 Dec;92(2):437-41. doi: 10.1111/j.1432-1033.1978.tb12764.x.
2
Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains.
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Reversible unfolding of the beta 2 subunit of Escherichia coli tryptophan synthetase and its proteolytic fragments.
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Comparison of denaturation of tryptophan synthase alpha-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid.
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5
Renaturation of guanidine-unfolded tryptophan synthase by multi-mixing stopped-flow dilution in D2O.
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Denaturation of uridine phosphorylase from Escherichia coli K-12 by guanidine hydrochloride.
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Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit.色氨酸合成酶α亚基保守脯氨酸突变体的去折叠和重折叠的平衡及动力学分析。
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Effect of single amino acid substitutions at the same position on stability of a two-domain protein.同一位置的单个氨基酸替换对双结构域蛋白质稳定性的影响。
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Kinetic characterization of early intermediates in the folding of E. coli tryptophan-synthase beta 2 subunit.大肠杆菌色氨酸合成酶β2亚基折叠过程中早期中间体的动力学特征
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Reconstitution of the isolated beta2-subunit of tryptophan synthase from Escherichia coli after dissociation induced by high hydrostatic pressure. Equilibrium and kinetic studies.
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