Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR

作者:Neto S E; Fonseca B M; Maycock C; Louro R O*
来源:Chemical Communications, 2014, 50(35): 4561-4563.
DOI:10.1039/c3cc49135h

摘要

Residual dipolar couplings measured by NMR spectroscopy reveal that the rhombicity of the electronic structure of low-spin paramagnetic hemes determines their relative contribution to the preferential orientation of a protein with multiple hemes when placed in a strong magnetic field.

  • 出版日期2014