JBIC Journal of Biological Inorganic Chemistry

, Volume 17, Issue 1, pp 71–79

Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures

Original Paper

DOI: 10.1007/s00775-011-0830-7

Cite this article as:
Sgrignani, J. & Pierattelli, R. J Biol Inorg Chem (2012) 17: 71. doi:10.1007/s00775-011-0830-7


Nuclear magnetic resonance (NMR) chemical shifts are experimental observables that are available during the first stage of the protein structure determination process. Recently, some methodologies for building structural models of proteins using only these experimental data have been implemented. To assess the potential of these methods for modeling metalloproteins (generally considered a challenging benchmark), we determined the structures of the yeast copper chaperone Atx1 and the CuA domain of Thermus thermophilus cytochrome c oxidase starting from the available chemical shift data. The metal centers were modeled using molecular dynamics simulations with molecular mechanics potentials. The results obtained are evaluated and discussed.


Chemical shift Molecular modeling Molecular dynamics Metalloprotein 

Copyright information

© SBIC 2011

Authors and Affiliations

  1. 1.Magnetic Resonance Center (CERM) and Department of Chemistry “Ugo Schiff”University of FlorenceSesto FiorentinoItaly
  2. 2.CNR-IOM-DEMOCRITOS National Simulation Center at SISSATriesteItaly

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