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.

ABSTRACT: Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate ¹³ C and ¹⁵ N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for ¹⁵ N atoms. Here we compare experimentally determined backbone ¹³ C^α and ¹⁵ N^H 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 ¹⁵ N^H chemical shift anisotropy values was obtained using the Amber ff15ipq for

SUBMITTER: Kraus J 

PROVIDER: S-EPMC8080305 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature