NMR chemical shift data and ab initio shielding calculations: Emerging tools for protein structure determination

F. A A Mulder; Michael Filatov

doi:10.1039/b811366c

NMR chemical shift data and ab initio shielding calculations: Emerging tools for protein structure determination

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Abstract

In this tutorial review, we discuss the utilization of chemical shift information as well as ab initio calculations of nuclear shieldings for protein structure determination. Both the empirical and computational aspects of the chemical shift are reviewed and the role of molecular dynamics and the accuracy of different computational methods are discussed. It is anticipated that incorporating theoretical information on chemical shifts will increase the accuracy of protein structures, in the solid and liquid state alike, and extend the applicability of NMR spectroscopy to ever larger systems.

Original language	English
Journal	Chemical Society Reviews
Volume	39
Issue	2
Pages (from-to)	578-590
Number of pages	13
ISSN	0306-0012
DOIs	https://doi.org/10.1039/b811366c
Publication status	Published - 8 Feb 2010
Externally published	Yes

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Cite this

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abstract = "In this tutorial review, we discuss the utilization of chemical shift information as well as ab initio calculations of nuclear shieldings for protein structure determination. Both the empirical and computational aspects of the chemical shift are reviewed and the role of molecular dynamics and the accuracy of different computational methods are discussed. It is anticipated that incorporating theoretical information on chemical shifts will increase the accuracy of protein structures, in the solid and liquid state alike, and extend the applicability of NMR spectroscopy to ever larger systems.",

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AB - In this tutorial review, we discuss the utilization of chemical shift information as well as ab initio calculations of nuclear shieldings for protein structure determination. Both the empirical and computational aspects of the chemical shift are reviewed and the role of molecular dynamics and the accuracy of different computational methods are discussed. It is anticipated that incorporating theoretical information on chemical shifts will increase the accuracy of protein structures, in the solid and liquid state alike, and extend the applicability of NMR spectroscopy to ever larger systems.

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