天然二硫键在溶菌酶折叠过程中极大地加速了二级结构的形成。
Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme.
作者信息
Goldberg M E, Guillou Y
机构信息
Unité de Biochimie Cellulaire, CNRS URA 1129, Institut Pasteur, Paris, France.
出版信息
Protein Sci. 1994 Jun;3(6):883-7. doi: 10.1002/pro.5560030603.
Abstract
To assess the respective roles of local and long-range interactions during protein folding, the influence of the native disulfide bonds on the early formation of secondary structure was investigated using continuous-flow circular dichroism. Within the first 4 ms of folding, lysozyme with intact disulfide bonds already had a far-UV CD spectrum reflecting large amounts of secondary structure. Conversely, reduced lysozyme remained essentially unfolded at this early folding time. Thus, native disulfide bonds not only stabilize the cfinal conformation of lysozyme but also provide, in early folding intermediates, the necessary stabilization that favors the formation of secondary structure.
摘要
为了评估蛋白质折叠过程中局部和长程相互作用的各自作用，使用连续流动圆二色性研究了天然二硫键对二级结构早期形成的影响。在折叠的最初4毫秒内，具有完整二硫键的溶菌酶已经具有反映大量二级结构的远紫外圆二色光谱。相反，还原型溶菌酶在这个早期折叠阶段基本上仍未折叠。因此，天然二硫键不仅稳定了溶菌酶的最终构象，而且在早期折叠中间体中提供了有利于二级结构形成的必要稳定性。
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本文引用的文献
1
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Biochemistry. 1981 Sep 29;20(20):5744-54. doi: 10.1021/bi00523a017.
2
Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor.亚稳态天然样双二硫键物种在牛胰蛋白酶抑制剂折叠转变中的动力学作用
J Mol Biol. 1984 Nov 5;179(3):497-526. doi: 10.1016/0022-2836(84)90077-9.
3
Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin.溶菌酶和α-乳白蛋白中瞬时折叠中间体的比较。
Biochemistry. 1985 Feb 12;24(4):874-81. doi: 10.1021/bi00325a010.
4
Disulphide bonds and protein stability.二硫键与蛋白质稳定性
Bioessays. 1988 Feb-Mar;8(2):57-63. doi: 10.1002/bies.950080204.
5
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6
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J Mol Biol. 1989 Feb 20;205(4):737-50. doi: 10.1016/0022-2836(89)90318-5.
7
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8
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Biochem J. 1991 Jan 1;273(Pt 1)(Pt 1):211-7. doi: 10.1042/bj2730211.
9
Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor.一个亚结构域在牛胰蛋白酶抑制剂折叠中的作用
Nature. 1990 Apr 12;344(6267):685-8. doi: 10.1038/344685a0.
10
The folding of hen lysozyme involves partially structured intermediates and multiple pathways.鸡溶菌酶的折叠涉及部分结构化的中间体和多种途径。
Nature. 1992 Jul 23;358(6384):302-7. doi: 10.1038/358302a0.
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