These authors contributed equally to this work.
1439-7633/asset/2268_left.gif?v=1&s=307233408e54255dc0d91f8b45dbcbc9d91c02fb)
1439-7633/asset/2268_right.gif?v=1&s=3d91b10da22cd11de4d8c9a972145ff16791ee1f)
Communication
In Situ Monitoring of Backbone Thioester Exchange by 19F NMR
Article first published online: 30 JUL 2009
DOI: 10.1002/cbic.200900380
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Pomerantz, W. C., Hadley, E. B., Fry, C. G. and Gellman, S. H. (2009), In Situ Monitoring of Backbone Thioester Exchange by 19F NMR. ChemBioChem, 10: 2177–2181. doi: 10.1002/cbic.200900380
- †
These authors contributed equally to this work.
Publication History
- Issue published online: 27 AUG 2009
- Article first published online: 30 JUL 2009
- Manuscript Received: 19 JUN 2009
Funded by
- NIH. Grant Number: GM061238
- Nanoscale Science and Engineering Center. Grant Number: NSF DMR-0425880
Keywords:
- backbone thioester exchange;
- coiled coil;
- fluorine;
- NMR spectroscopy;
- protein folding
19F NMR to monitor BTE: A new strategy for assessing polypeptide tertiary structural stability by using thiol–thioester exchange is described. The backbone thioester exchange (BTE) method has previously been used to evaluate fold stability with HPLC measurements. Here we show that BTE can be followed by 19F NMR, which offers technical advantages. This technique was used for rapid identification of the most stable antiparallel coiled coil in a small library of new sequences.