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Amyloid Hydrogen Bo...
Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
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- Wei, Juan (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
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- Antzutkin, Oleg (author)
- Luleå tekniska universitet,Kemiteknik
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- Filippov, Andrei (author)
- Luleå tekniska universitet,Kemiteknik
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- Iuga, Dinu (author)
- Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
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- Lam, Pui Yiu (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
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- Barrow, Mark P. (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
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- Dupree, Ray (author)
- University of Warwick, Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
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- Brown, Steven P. (author)
- Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
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- O'Connor, Peter B. (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
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(creator_code:org_t)
- 2016-04-01
- 2016
- English.
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In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 55:14, s. 2065-2068
- Related links:
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https://pubs.acs.org...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- A combined approach, using Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) and solid-state NMR (Nuclear Magnetic Resonance), shows a high degree of polymorphism exhibited by Aβ species in forming hydrogen-bonded networks. Two Alzheimer’s Aβ peptides, Ac-Aβ16–22-NH2 and Aβ11–25, selectively labeled with 17O and 15N at specific amino acid residues were investigated. The total amount of peptides labeled with 17O as measured by FTICR-MS enabled the interpretation of dephasing observed in 15N{17O}REAPDOR solid-state NMR experiments. Specifically, about one-third of the Aβ peptides were found to be involved in the formation of a specific >C═17O···H–15N hydrogen bond with their neighbor peptide molecules, and we hypothesize that the rest of the molecules undergo ± n off-registry shifts in their hydrogen bonding networks.
Subject headings
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Keyword
- Chemistry of Interfaces
- Gränsytors kemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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