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Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Wei, Juan (författare)
Department of Chemistry and Department of Physics, University of Warwick, Coventry
Antzutkin, Oleg (författare)
Luleå tekniska universitet,Kemiteknik
Filippov, Andrei (författare)
Luleå tekniska universitet,Kemiteknik
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Iuga, Dinu (författare)
Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
Lam, Pui Yiu (författare)
Department of Chemistry and Department of Physics, University of Warwick, Coventry
Barrow, Mark P. (författare)
Department of Chemistry and Department of Physics, University of Warwick, Coventry
Dupree, Ray (författare)
University of Warwick, Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
Brown, Steven P. (författare)
Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
O'Connor, Peter B. (författare)
Department of Chemistry and Department of Physics, University of Warwick, Coventry
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 (creator_code:org_t)
2016-04-01
2016
Engelska.
Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 55:14, s. 2065-2068
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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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.

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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