Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5.

ABSTRACT: There is considerable interest in determining amide-(15)N chemical shift anisotropy (CSA) tensors from biomolecules and understanding their variation for structural and dynamics studies using solution and solid-state NMR spectroscopy and also by quantum chemical calculations. Due to the difficulties associated with the measurement of CSA tensors from membrane proteins, NMR-based structural studies heavily relied on the CSA tensors determined from model systems, typically single crystals of model peptides. In the present study, the principal components of backbone amide-(15)N CSA tensors have been determined using density functional theory for a 16.7 kDa membrane-bound paramagnetic heme containing protein, cytochrome-b(5) (cytb(5)). All the calculations were performed by taking residues wit

SUBMITTER: Pandey MK 

PROVIDER: S-EPMC3564578 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature