Accurate Backbone 13C and 15N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM : Details of Structure and Environment Matter
(2020) In ChemPhysChem 21(13). p.1436-1443- Abstract
Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate 13C and 15N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for 15N atoms. Here we compare experimentally determined backbone 13Cα and 15NH 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 15NH chemical shift anisotropy... (More)
Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate 13C and 15N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for 15N atoms. Here we compare experimentally determined backbone 13Cα and 15NH 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 15NH 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.
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- author
- Kraus, Jodi ; Gupta, Rupal ; Lu, Manman ; Gronenborn, Angela M. ; Akke, Mikael LU and Polenova, Tatyana
- organization
- publishing date
- 2020-07-02
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Chemical shift anisotropy, microcrystalline protein, QM/MM, recoupling, solid-state NMR
- in
- ChemPhysChem
- volume
- 21
- issue
- 13
- pages
- 8 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:85085997223
- pmid:32363727
- ISSN
- 1439-4235
- DOI
- 10.1002/cphc.202000249
- language
- English
- LU publication?
- yes
- id
- b356855b-0feb-4f71-a945-0dcd9919e4fb
- date added to LUP
- 2020-06-30 15:47:53
- date last changed
- 2024-08-21 23:53:42
@article{b356855b-0feb-4f71-a945-0dcd9919e4fb, abstract = {{<p>Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate <sup>13</sup>C and <sup>15</sup>N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for <sup>15</sup>N atoms. Here we compare experimentally determined backbone <sup>13</sup>C<sup>α</sup> and <sup>15</sup>N<sup>H</sup> 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 <sup>15</sup>N<sup>H</sup> 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.</p>}}, author = {{Kraus, Jodi and Gupta, Rupal and Lu, Manman and Gronenborn, Angela M. and Akke, Mikael and Polenova, Tatyana}}, issn = {{1439-4235}}, keywords = {{Chemical shift anisotropy; microcrystalline protein; QM/MM; recoupling; solid-state NMR}}, language = {{eng}}, month = {{07}}, number = {{13}}, pages = {{1436--1443}}, publisher = {{John Wiley & Sons Inc.}}, series = {{ChemPhysChem}}, title = {{Accurate Backbone <sup>13</sup>C and <sup>15</sup>N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM : Details of Structure and Environment Matter}}, url = {{http://dx.doi.org/10.1002/cphc.202000249}}, doi = {{10.1002/cphc.202000249}}, volume = {{21}}, year = {{2020}}, }