In situ solid-state NMR spectroscopy of protein in heterogeneous membranes: the baseplate antenna complex of Chlorobaculum tepidum

Natalia V Kulminskaya; Marie Ø Pedersen; Morten Bjerring; Jarl Underhaug; Mette Miller; Niels-Ulrik Frigaard; Jakob T Nielsen; Niels Chr Nielsen

doi:10.1002/anie.201201160

In situ solid-state NMR spectroscopy of protein in heterogeneous membranes: the baseplate antenna complex of Chlorobaculum tepidum

Angew Chem Int Ed Engl. 2012 Jul 9;51(28):6891-5. doi: 10.1002/anie.201201160. Epub 2012 Jun 8.

Authors

Natalia V Kulminskaya¹, Marie Ø Pedersen, Morten Bjerring, Jarl Underhaug, Mette Miller, Niels-Ulrik Frigaard, Jakob T Nielsen, Niels Chr Nielsen

Affiliation

¹ Department of Chemistry, University of Aarhus, Denmark.

PMID: 22685072
DOI: 10.1002/anie.201201160

Abstract

A clever combination: an in situ solid-state NMR analysis of CsmA proteins in the heterogeneous environment of the photoreceptor of Chlorobaculum tepidum is reported. Using different combinations of 2D and 3D solid-state NMR spectra, 90 % of the CsmA resonances are assigned and provide on the basis of chemical shift data information about the structure and conformation of CsmA in the CsmA-bacteriochlorophyll a complex.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism*
Bacteriochlorophyll A / metabolism*
Cell Membrane / metabolism*
Chlorobi / metabolism*
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Conformation
Protein Conformation

Substances

Bacterial Proteins
Bacteriochlorophyll A
CsmA protein, Chlorobium tepidum