Please use this identifier to cite or link to this item: https://doi.org/10.1007/s10858-011-9549-6
Title: Measurement of amide hydrogen exchange rates with the use of radiation damping
Authors: Fan, J.-S. 
Lim, J.
Yu, B.
Yang, D. 
Keywords: Amide hydrogen exchange
Conformational change
Protein dynamics
Protein structure
Radiation damping
Issue Date: Sep-2011
Source: Fan, J.-S., Lim, J., Yu, B., Yang, D. (2011-09). Measurement of amide hydrogen exchange rates with the use of radiation damping. Journal of Biomolecular NMR 51 (1-2) : 151-162. ScholarBank@NUS Repository. https://doi.org/10.1007/s10858-011-9549-6
Abstract: A simple method for measuring amide hydrogen exchange rates is presented, which is based on the selective inversion of water magnetization with the use of radiation damping. Simulations show that accurate exchange rates can be measured despite the complications of radiation damping and cross relaxation to the exchange process between amide and water protons. This method cannot eliminate the contributions of the exchange-relayed NOE and direct NOE to the measured exchange rates, but minimize the direct NOE contribution. In addition, the amides with a significant amount of such indirect contributions are possible to be identified from the shape of the exchange peak intensity profiles or/and from the apparent relaxation rates of amide protons which are extracted from fitting the intensity profiles to an equation established here for our experiment. The method was tested on ubiquitin and also applied to an acyl carrier protein. The amide exchange rates for the acyl carrier protein at two pHs indicate that the entire protein is highly dynamic on the second timescale. Low protection factors for the residues in the regular secondary structural elements also suggest the presence of invisible unfolded species. The highly dynamic nature of the acyl carrier protein may be crucial for its interactions with its substrate and enzymes. © 2011 Springer Science+Business Media B.V.
Source Title: Journal of Biomolecular NMR
URI: http://scholarbank.nus.edu.sg/handle/10635/101066
ISSN: 09252738
DOI: 10.1007/s10858-011-9549-6
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