Prion Protein Amyloid Formation Involves Structural Rearrangements in the C-Terminal Domain

被引：18
|
作者：
Kumar, Jitendra [1 ]
Sreeramulu, Sridhar [1 ]
Schmidt, Thorsten L.
Richter, Christian [1 ]
Vonck, Janet [2 ]
Heckel, Alexander
Glaubitz, Clemens [3 ]
Schwalbe, Harald [1 ]
机构：
[1] Goethe Univ Frankfurt, Inst Organ Chem & Chem Biol, Ctr Biomol Magnet Resonance BMRZ, D-60438 Frankfurt, Germany
[2] Max Planck Inst Biophys, Dept Biol Struct, D-60438 Frankfurt, Germany
[3] Goethe Univ Frankfurt, Inst Biophys Chem, Ctr Biomol Magnet Resonance BMRZ, D-60438 Frankfurt, Germany
来源：
CHEMBIOCHEM | 2010年 / 11卷 / 09期
关键词：
aggregation; amyloid beta-peptides; misfolding; NMR spectroscopy; prions; TRIPLE-RESONANCE EXPERIMENTS; NMR STRUCTURE; HYDROGEN/DEUTERIUM EXCHANGE; ELECTRON CRYSTALLOGRAPHY; PEPTIDE; 106-126; MOLECULAR-BASIS; BETA-SHEET; FIBRILS; AGGREGATION; SCRAPIE;
D O I：
10.1002/cbic.201000076
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Hard core: We have analyzed the structural rearrangements of the urea-denatured state of recombinant prion protein by using liquid-state NMR spectroscopy. Our studies document that prion amyloid fibrils generated from monomeric, urea-unfolded human prion protein have a rigid core between residues 145-223. (Graph Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：1208 / 1213
页数：6
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