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Conformational Swit...
Conformational Switching in PolyGln Amyloid Fibrils Resulting from a Single Amino Acid Insertion
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- Huang, Rick K. (författare)
- Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland
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- Baxa, Ulrich (författare)
- Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland
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- Aldrian, Gudrun (författare)
- Centre de Recherches de Biochimie Macromoléculaire, CNRS, University of Montpellier 1 and 2
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- Ahmed, Abdullah B. (författare)
- Centre de Recherches de Biochimie Macromoléculaire, CNRS, University of Montpellier 1 and 2
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- Wall, Joseph P. (författare)
- Department of Biology, Brookhaven National Laboratory, Upton New York
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- Mizuno, Naoko (författare)
- Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland
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- Antzutkin, Oleg (författare)
- Luleå tekniska universitet,Kemiteknik
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- Steven, Alasdair C. (författare)
- Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland
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- Kajava, Andrey V. (författare)
- Centre de Recherches de Biochimie Macromoléculaire, CNRS, University of Montpellier 1 and 2
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(creator_code:org_t)
- Elsevier BV, 2014
- 2014
- Engelska.
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Ingår i: Biophysical Journal. - : Elsevier BV. - 0006-3495 .- 1542-0086. ; 106:10, s. 2134-2142
- Relaterad länk:
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http://www.cell.com/...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The established correlation between neurodegenerative disorders and intracerebral deposition of polyglutamine aggregates motivates attempts to better understand their fibrillar structure. We designed polyglutamines with a few lysines inserted to overcome the hindrance of extreme insolubility and two D-lysines to limit the lengths of β-strands. One is 33 amino acids long (PolyQKd-33) and the other has one fewer glutamine (PolyQKd-32). Both form well-dispersed fibrils suitable for analysis by electron microscopy. Electron diffraction confirmed cross-β structures in both fibrils. Remarkably, the deletion of just one glutamine residue from the middle of the peptide leads to substantially different amyloid structures. PolyQKd-32 fibrils are consistently 10–20% wider than PolyQKd-33, as measured by negative staining, cryo-electron microscopy, and scanning transmission electron microscopy. Scanning transmission electron microscopy analysis revealed that the PolyQKd-32 fibrils have 50% higher mass-per-length than PolyQKd-33. This distinction can be explained by a superpleated β-structure model for PolyQKd-33 and a model with two β-solenoid protofibrils for PolyQKd-32. These data provide evidence for β-arch-containing structures in polyglutamine fibrils and open future possibilities for structure-based drug design.
Ämnesord
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Nyckelord
- Chemistry of Interfaces
- Gränsytors kemi
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- art (ämneskategori)
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