富含脯氨酸的全β折叠纤连蛋白III型结构域的快速重折叠。
Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.
作者信息
Plaxco K W, Spitzfaden C, Campbell I D, Dobson C M
机构信息
Oxford Centre for Molecular Sciences, University of Oxford, England.
出版信息
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10703-6. doi: 10.1073/pnas.93.20.10703.
Abstract
Fibronectin type III modules contain approximately 90 residues and are an extremely common building block of animal proteins. Despite containing a complex all-beta-sheet topology and eight prolines, the refolding of the 10th type III module of human fibronectin has been found to be very rapid, with native core packing, amide hydrogen bonding, and backbone conformation all recovered within 1 s at 5 degrees C. These observations indicate that this domain can overcome many structural characteristics often thought to slow the folding process.
摘要
III型纤连蛋白模块包含大约90个残基，是动物蛋白中极为常见的结构单元。尽管含有复杂的全β折叠拓扑结构和八个脯氨酸，但已发现人纤连蛋白第10个III型模块的重折叠非常迅速，在5摄氏度下1秒内即可恢复天然的核心堆积、酰胺氢键和主链构象。这些观察结果表明，该结构域可以克服许多通常被认为会减缓折叠过程的结构特征。
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