NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation
Article first published online: 23 DEC 2013
© 2013 The Protein Society
Volume 23, Issue 2, pages 167–178, February 2014
How to Cite
Garrison, M. A. and Crowhurst, K. A. (2014), NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation. Protein Science, 23: 167–178. doi: 10.1002/pro.2402
- Issue published online: 22 JAN 2014
- Article first published online: 23 DEC 2013
- Accepted manuscript online: 4 DEC 2013 12:55AM EST
- Manuscript Accepted: 2 DEC 2013
- Manuscript Revised: 1 DEC 2013
- Manuscript Received: 9 NOV 2013
- NSF. Grant Number: CHE-1040134
- College of Science and Mathematics at CSU Northridge
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