A Concept for Rapid Protein‐Structure Determination by Solid‐State NMR Spectroscopy

Abstract

The three-dimensional fold of an immobilized polypeptide is predicted at atomic resolution from solid-state NMR spectroscopic data (see picture) obtained for a single uniformly [13C,15N] isotope labeled sample. The method involves the combined analysis of conformation-dependent NMR frequencies and short 1H–1H distances and may lead to the rapid characterization of three-dimensional protein structures. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2005/z462516_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.