Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.

Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.
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G 蛋白 B1 结构域的突变可延迟体外淀粉样原纤维形成的发生。

DOI:
10.1110/ps.0227403
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发表时间:
2003
期刊:
Protein science : a publication of the Protein Society.
影响因子:
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通讯作者:
Regan,Lynne
Regan,Lynne
中科院分区:
--
文献类型:
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作者:
Ramirez-Alvarado,Marina;Cocco,MelanieJ;Regan,Lynne

文献摘要

相似文献

We previously reported that under certain experimental conditions, many variants of the B1 domain of IgG‐binding protein G fromStreptococcusform fibrils reproducibly. The variant I6T53 was the focus of the present study because the lag phase in the kinetics of fibril formation by this variant is significantly longer than that of other variants. This lag phase is distinguished by changes in both intrinsic fluorescence intensity and in light scattering of the protein. NMR diffusion measurements suggest that the soluble protein during the lag phase is monomeric. The kinetic profiles of fibril formation are found to depend on experimental conditions. The first kinetic phase diminishes almost completely when the reaction is seeded with preformed amyloid fibrils.