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

页码：1208 / 1213

页数：6

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