Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
 

Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.

Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.

Magn Reson Chem. 2011 Feb;49(2):65-9

Authors: Middleton DA

Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary structure, alignment and registration of ?-strands within amyloid fibrils and identify the tertiary and quaternary contacts defining the packing of the ?-sheet layers. Detection of (14) N?(13) C dipolar couplings may provide potentially useful additional structural constraints on ?-sheet packing within amyloid fibrils but has not until now been exploited for this purpose. Here a frequency-selective, transfer of population in double resonance SSNMR experiment is used to detect a weak (14) N?(13) C dipolar coupling in amyloid-like fibrils of the peptide H(2) N-SNNFGAILSS-COOH, which was uniformly (13) C and (15) N labelled across the four C-terminal amino acids. The (14) N?(13) C interatomic distance between leucine and asparagine side groups is constrained between 2.4 and 3.8 Å, which allows current structural models of the ?-spine arrangement within the fibrils to be refined. This procedure could be useful for the general structural analysis of other proteins in condensed phases and environments, such as biological membranes. Copyright © 2011 John Wiley & Sons, Ltd.

PMID: 21254226 [PubMed - in process]



Source: PubMed