uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Combined Solution- and Magic Angle Spinning NMR Reveals Regions of Distinct Dynamics in Amyloid beta Protofibrils
Swedish Univ Agr Sci SLU, Dept Chem & Biotechnol, Uppsala, Sweden.;KTH Royal Inst Technol, Dept Chem, Stockholm, Sweden..
Umea Univ, Dept Chem, Umea, Sweden..
Univ Gothenburg, Swedish NMR Ctr, Gothenburg, Sweden..
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Swedish Univ Agr Sci SLU, Dept Chem & Biotechnol, Uppsala, Sweden..
Show others and affiliations
2016 (English)In: CHEMISTRYSELECT, ISSN 2365-6549, Vol. 1, no 18, p. 5850-5853Article in journal (Refereed) Published
Abstract [en]

Solid-state magic angle spinning (MAS) NMR has emerged as an important tool for investigations of protein aggregates and amyloid fibrils, which are not accessible for solution NMR experiments. We recently presented a structural model for amyloid beta (A beta) protofibrils based on MAS-NMR data. The absence of resonances for the N-terminus of A beta in this dataset suggested that it might be disordered and more dynamic than the structural core. We here provide evidence for a distinct dynamic regime in the N-terminal part of the peptide and show that the structural characteristics of this region can be elucidated using C-13-detected solution NMR. The results shed more light on the structural properties of pre-fibrillar A beta species and demonstrate the potential of combining MAS and solution NMR experiments for the characterization of structure and dynamics of complex protein assemblies.

Place, publisher, year, edition, pages
WILEY-V C H VERLAG GMBH , 2016. Vol. 1, no 18, p. 5850-5853
Keywords [en]
Amyloid beta, protofibrils, solid-state NMR, solution NMR
National Category
Chemical Sciences Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-320822DOI: 10.1002/slct.201601468ISI: 000395427600038OAI: oai:DiVA.org:uu-320822DiVA, id: diva2:1091127
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationAvailable from: 2017-04-26 Created: 2017-04-26 Last updated: 2017-04-26Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full text
By organisation
Department of Cell and Molecular Biology
Chemical SciencesBiochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 189 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf