Search: WFRF:(Barrow Mark P.)
> (2016) >
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
-
- Wei, Juan (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
- Antzutkin, Oleg (author)
- Luleå tekniska universitet,Kemiteknik
-
- Filippov, Andrei (author)
- Luleå tekniska universitet,Kemiteknik
-
show more...
-
- Iuga, Dinu (author)
- Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
- Lam, Pui Yiu (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
- Barrow, Mark P. (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
- Dupree, Ray (author)
- University of Warwick, Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
- Brown, Steven P. (author)
- Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
- O'Connor, Peter B. (author)
- Department of Chemistry and Department of Physics, University of Warwick, Coventry
-
show less...
-
(creator_code:org_t)
- 2016-04-01
- 2016
- English.
-
In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 55:14, s. 2065-2068
- Related links:
-
https://pubs.acs.org...
-
show more...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- 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)
Find in a library
To the university's database