Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated

Tomonori Mishima, Takatoshi Ohkuri, Akira Monji, Taiji Imoto, Tadashi Ueda

研究成果: Contribution to journalArticle査読

16 被引用数 (Scopus)

抄録

Reduced hen lysozyme has a residual structure involving long-range interaction. It has been demonstrated that a single mutation (A9G, W62G, W111G, or W123G) in the residual structure differently modulates the long-range interactions of reduced lysozyme. To examine whether such variations in the residual structure affect amyloid formation, reduced and alkylated mutant lysozymes were incubated under the amyloid-fibrillation condition. From the analyses of CD spectra and thioflavine T fluorescences, it was suggested that variation in residual structure led to different amyloid formation. Interestingly, the extent of amyloid formation did not always correlate with the extent to which the residual structure was maintained, resulting in the involvement of a hydrophobic cluster normally contained in W111 in the reduced lysozyme. Published by Cold Spring Harbor Laboratory Press.

本文言語英語
ページ(範囲)2448-2452
ページ数5
ジャーナルProtein Science
15
10
DOI
出版ステータス出版済み - 2006

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学

フィンガープリント

「Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated」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