caa a22 4500 445325518 CHVBK 20180317142719.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s10858-011-9549-6 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9549-6 Measurement of amide hydrogen exchange rates with the use of radiation damping [Elektronische Daten] [Jing-Song Fan, Jackwee Lim, Binhan Yu, Daiwen Yang] 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. Springer Science+Business Media B.V., 2011 Amide hydrogen exchange nationallicence Protein dynamics nationallicence Protein structure nationallicence Conformational change nationallicence Radiation damping nationallicence Fan Jing-Song Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut Lim Jackwee Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut Yu Binhan Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut Yang Daiwen Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 151-162 0925-2738 51:1-2<151 2011 51 10858 https://doi.org/10.1007/s10858-011-9549-6 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9549-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Fan Jing-Song Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut NATIONALLICENCE 700 1- Lim Jackwee Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut NATIONALLICENCE 700 1- Yu Binhan Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut NATIONALLICENCE 700 1- Yang Daiwen Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 151-162 0925-2738 51:1-2<151 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer