Mechanical Unfoldons as Building Blocks of Maltose-binding Protein

Morten Bertz, Matthias Rief*

*この研究の対応する著者

研究成果: Article査読

63 被引用数 (Scopus)

抄録

Identifying independently folding cores or substructures is important for understanding and assaying the structure, function and assembly of large proteins. Here, we suggest mechanical stability as a criterion to identify building blocks of the 366 amino acid maltose-binding protein (MBP). We find that MBP, when pulled at its termini, unfolds via three (meta-) stable unfolding intermediates. Consequently, the MBP structure consists of four structural blocks (unfoldons) that detach sequentially from the folded structure upon force application. We used cysteine cross-link mutations to characterize the four unfoldons structurally. We showed that many MBP constructs composed of those building blocks indeed form stably folded structures in solution. Mechanical unfoldons may provide a new tool for a systematic search for stable substructures of large proteins.

本文言語English
ページ(範囲)447-458
ページ数12
ジャーナルJournal of Molecular Biology
378
2
DOI
出版ステータスPublished - 2008 4月 25
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

フィンガープリント

「Mechanical Unfoldons as Building Blocks of Maltose-binding Protein」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル