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

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)4561-4563
Number of pages3
JournalChemical Communications
Volume50
Issue number35
DOIs
Publication statusPublished - 7 May 2014

Fingerprint

Dive into the research topics of 'Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR'. Together they form a unique fingerprint.

Cite this