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

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

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2448-2452
Number of pages5
JournalProtein Science
Volume15
Issue number10
DOIs
Publication statusPublished - 2006

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated'. Together they form a unique fingerprint.

Cite this