Sequence and structure analysis of parallel beta helices: Implication for constructing amyloid structural models

Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/34236

Title:	Sequence and structure analysis of parallel beta helices: Implication for constructing amyloid structural models
Authors:	Tsai HH,Gunasekaran K,Nussinov R.
Contributors:	化學研究所
Keywords:	SOLID-STATE NMR;SHEET STRUCTURE;SECONDARY STRUCTURE;MOLECULAR-DYNAMICS;ANTIFREEZE PROTEIN;ENERGY LANDSCAPE;FIBRIL FORMATION;PRION PROTEIN;PEPTIDE;AGGREGATION
Date:	2006
Issue Date:	2010-07-07 12:00:15 (UTC+8)
Publisher:	中央大學
Abstract:	Increasing evidence suggests that amyloids and parallel beta helices may share similar motifs. A systemic analysis of beta helices is performed to examine their sequence and structural characteristics. lie prefers to occur in beta strands. In contrast, Pr
Relation:	STRUCTURE
Appears in Collections:	[Graduate Institute of Chemistry] journal & Dissertation

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