Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter

Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate C and N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly...

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Bibliographic Details
Published in:Chemphyschem 2020-07, Vol.21 (13), p.1436-1443
Main Authors: Kraus, Jodi, Gupta, Rupal, Lu, Manman, Gronenborn, Angela M, Akke, Mikael, Polenova, Tatyana
Format: Article
Language:English
Subjects:
Blood Proteins - chemistry
Carbon Isotopes - chemistry
Density Functional Theory
Galectins - chemistry
Humans
Models, Chemical
Molecular Dynamics Simulation
Nitrogen Isotopes - chemistry
Nuclear Magnetic Resonance, Biomolecular
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Summary:Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate C and N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for N atoms. Here we compare experimentally determined backbone C and N chemical shift tensors by MAS NMR with hybrid quantum mechanics/molecular mechanics/molecular dynamics (MD-QM/MM) calculations for the carbohydrate-binding domain of galectin-3. Excellent agreement between experimental and computed N chemical shift anisotropy values was obtained using the Amber ff15ipq force field when solvent dynamics was taken into account in the calculation. Our results establish important benchmark conditions for improving the accuracy of chemical shift calculations in proteins and may aid in the validation of protein structure models derived by MAS NMR.
ISSN:1439-4235
1439-7641
DOI:10.1002/cphc.202000249