Conformational Flexibility of Aggregation-Prone Peptides Studied By PET-FCS

被引：0

作者：

Doose, Soeren ^{[1
]}

Loellmann, Marc ^{[2
]}

Schwering, Michael ^{[3
]}

Sauer, Markus ^{[1
]}

机构：

[1] Univ Wurzburg, D-97070 Wurzburg, Germany

[2] Univ Bielefeld, D-33615 Bielefeld, Germany

[3] Heidelberg Univ, Heidelberg, Germany

来源：

BIOPHYSICAL JOURNAL | 2010年 / 98卷 / 03期

关键词：

D O I：

10.1016/j.bpj.2009.12.264

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

引用

页码：46A / 46A

页数：1

共 26 条

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[24] Tertiary Butanol Induced Amyloidogenesis of Hen Egg White Lysozyme (HEWL) Is Facilitated by Aggregation-Prone Alkali-Induced Molten Globule Like Conformational State
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[25] Early events in protein aggregation: Molecular flexibility and hydrophobicity/charge interaction in amyloid peptides as studied by molecular dynamics simulations
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Manetti, C
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PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2005, 58 (01) : 110 - 118
[26] Synthesis and purification of aggregation-prone hydrophobic peptides by the incorporation of an Fmoc dipeptide with the peptide bond protected with a modified 2-hydroxy-4-methoxybenzyl (Hmb) group
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TETRAHEDRON LETTERS, 2008, 49 (24) : 3921 - 3924

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