Simultaneous Assignment and Structure Determination of Protein Backbones by Using NMR Dipolar Couplings

Abstract

Running on automatic: Folds for proteins up to around 125 residues can be achieved rapidly and without manual intervention by integration of bioinformatics tools with NMR spectroscopy in dilute liquid-crystalline phases (see picture). Data intensive and time-consuming assignment of backbone resonances prior to structure determination is not required any more. This greatly accelerates structure determination of proteins by NMR spectroscopy. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2004/z53588_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.