The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here:

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Portrait of Sara Snogerup Linse

Sara Linse


Portrait of Sara Snogerup Linse

High Resolution Structural Characterization of A beta(42) Amyloid Fibrils by Magic Angle Spinning NMR


  • Michael T. Covin
  • Robert Silvers
  • Birgitta Frohm
  • Yongchao Su
  • Sara Linse
  • Robert G. Griffin

Summary, in English

The presence of amyloid plaques composed of amyloid beta (A beta) fibrils is a hallmark of Alzheimer's disease (AD). The A beta peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted A beta(1-40) and A beta(1-42), respectively. While there have been numerous reports that structurally characterize fibrils of A beta(1-40), very little is known about the structure of amyloid fibrils of A beta(1-42), which are considered the more toxic alloform involved in AD. We have prepared isotopically C-13/N-13 labeled A beta(M01-42) fibrils in vitro from recombinant protein and examined their C-13-C-13 and C-13-N-15 magic angle spinning (MAS) NMR spectra. In contrast to several other studies of A beta fibrils, we observe spectra with excellent resolution and a single set of chemical shifts, suggesting the presence of a single fibril morphology. We report the initial structural characterization of A beta(M01-42) fibrils utilizing C-13 and N-15 shift assignments of 38 of the 43 residues, including the backbone and side chains, obtained through a series of cross-polarization based 2D and 3D C-13-C-13, C-13-N-15 MAS NMR experiments for rigid residues along with J-based 2D TOBSY experiments for dynamic residues. We find that the first similar to 5 residues are dynamic and most efficiently detected in a J-based TOBSY spectrum. In contrast, residues 16-42 are easily observed in cross-polarization experiments and most likely form the amyloid core. Calculation of psi and phi dihedral angles from the chemical shift assignments indicate that beta-strands are present in the fibril's secondary structure.


  • Biochemistry and Structural Biology
  • MultiPark: Multidisciplinary research focused on Parkinson´s disease

Publishing year







Journal of the American Chemical Society





Document type

Journal article


The American Chemical Society (ACS)


  • Structural Biology




  • ISSN: 1520-5126