Journal of Biomolecular NMR

, Volume 55, Issue 1, pp 71–78 | Cite as

The protein amide 1HN chemical shift temperature coefficient reflects thermal expansion of the N–H···O=C hydrogen bond



The protein amide 1HN chemical shift temperature coefficient can be determined with high accuracy by recording spectra at different temperatures, but the physical mechanism responsible for this temperature dependence is not well understood. In this work, we find that this coefficient strongly correlates with the temperature coefficient of the through-hydrogen-bond coupling, 3hJNC′, based on NMR measurements of protein GB3. Parallel tempering molecular dynamics simulation suggests that the hydrogen bond distance variation at different temperatures/replicas is largely responsible for the 1HN chemical shift temperature dependence, from which an empirical equation is proposed to predict the hydrogen bond thermal expansion coefficient, revealing responses of individual hydrogen bonds to temperature changes. Different expansion patterns have been observed for various networks formed by β strands.


Amide proton GB3 Chemical shift temperature coefficient Molecular dynamics simulation Hydrogen bond 



The authors would like to thank Dr. Dennis Torchia for the critical reading of the manuscript and Shanghai supercomputer center for the computer resources. This work was supported in part by 100 Talent Project of Chinese Academy of Sciences, National Nature Science Foundation of China (Grant no. 21173247) and the Foundation for Outstanding Young Scientist in Shandong Province (Grant no. JQ201104).

Supplementary material

10858_2012_9689_MOESM1_ESM.docx (58 kb)
Supplementary material 1 (DOCX 57 kb)


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Copyright information

© Springer Science+Business Media Dordrecht 2012

Authors and Affiliations

  1. 1.Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess TechnologyChinese Academy of SciencesQingdaoChina

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