کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2030118 1071039 2006 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Amyloid Formation May Involve α- to β Sheet Interconversion via Peptide Plane Flipping
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Amyloid Formation May Involve α- to β Sheet Interconversion via Peptide Plane Flipping
چکیده انگلیسی

SummaryThe toxic component of amyloid is not the mature fiber but a soluble prefibrillar intermediate. It has been proposed, from molecular dynamics simulations, that the precursor is composed of α sheet, which converts into the β sheet of mature amyloid via peptide plane flipping. α sheet, not seen in proteins, occurs as isolated stretches of polypeptide. We show that the α- to β sheet transition can occur by the flipping of alternate peptide planes. The flip can be described as αRαL↔ββ. A search conducted within sets of closely related protein crystal structures revealed that these flips are common, occurring in 8.5% of protein families. The average “αL” conformation found is in an adjacent and less populated region of the Ramachandran plot, as expected if the flanking peptide planes, being hydrogen bonded, are restricted in their movements. This work provides evidence for flips allowing direct α- to β sheet interconversion.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 14, Issue 9, September 2006, Pages 1369–1376
نویسندگان
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