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Published online before print September 8, 2006, 10.1110/ps.062258206
Protein Science (2006), 15:2448-2452. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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FOR THE RECORD

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

Tomonori Mishima1,4, Takatoshi Ohkuri1,4, Akira Monji2, Taiji Imoto3 and Tadashi Ueda1

1 Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan
2 Department of Neuropsychiatry, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan
3 Faculty of Biotechnology and Life Science, Sojo University, Kumamoto 860-0082, Japan

(RECEIVED April 4, 2006; FINAL REVISION June 11, 2006; ACCEPTED July 7, 2006)

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.

Keywords: lysozyme; amyloid formation; residual structure


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