R. Tycko, Biomolecular solid state NMR: Advances in structural methodology and applications to peptide and protein fibrils, ANN R PH CH, 52, 2001, pp. 575-606
Solid state nuclear magnetic resonance (NMR) methods can provide atomic-lev
el structural constraints on peptides and proteins in forms that are not am
enable to characterization by other high-resolution structural techniques,
owing to insolubility, high molecular weight, noncrystallinity, or other ch
aracteristics. Important examples include peptide and protein fibrils and m
embrane-bound peptides and proteins. Recent advances in solid state NMR met
hodology aimed at structural problems in biological systems are reviewed. T
he power of these methods is illustrated by experimental results on amyloid
fibrils and other protein fibrils.