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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chan, Jerry C. C. Cheng, Hsin-mei Chou, Fang-chieh Chang, Chi-fon Huang, Shing-jong Chen, Yun-ru Lin, Ni-shian Chao, John Ching-hao Chang, Yu-jen |
| Description | Author Affiliation: Lin NS ( Department of Chemistry, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei 106, Taiwan.) |
| Abstract | Amyloid fibrils are filamentous and insoluble forms of peptides or proteins. Proline has long been considered to be incompatible with the cross-β structural motif of amyloid fibrils. On the basis of solid-state NMR spectroscopy data, we present a structural model of an in-register parallel β sheet for the amyloid fibrils formed from a human prion protein fragment, $huPrP_{127–47}.$ We have developed a simple solid-state NMR spectroscopy technique to identify solvent-protected backbone amide protons in a H/D exchange experiment without disaggregating the amyloid fibrils, from which we find that proline residue $P_{137}$ does not disrupt the β-sheet structure from $G_{127}$ to $G_{142}.$ We suggest that the resultant kink at $P_{137}$ generates a twist between adjacent peptide strands to maintain hydrogen bonding in the β-sheet regions flanking the $P_{137}$ residue. Although proline can be well integrated into the cross-β structure of amyloid fibrils, the kink formed at the position of the proline residue will considerably weaken the hydrogen bonding between the neighboring strands, especially when the mutation site is near the central region of a β sheet. |
| ISSN | 09476539 |
| e-ISSN | 15213765 |
| Journal | Chemistry - A European Journal |
| Issue Number | 18 |
| Volume Number | 16 |
| Language | English |
| Publisher | Wiley-VCH;ChemPubSoc Europe |
| Publisher Date | 2010-05-10 |
| Publisher Place | Germany |
| Access Restriction | Open |
| Subject Keyword | Amyloid Beta-Peptides Chemistry Amyloid Peptide Fragments Prions Proline Amino Acid Sequence Metabolism Hydrogen Bonding Molecular Structure Nuclear Magnetic Resonance, Biomolecular Protein Conformation Quantum Theory Research Support, Non-U.S. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Catalysis |
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