Publication details
Backbone assignment and secondary structure of the PsbQ protein from Photosystem II
| Authors | |
|---|---|
| Year of publication | 2011 |
| Type | Article in Periodical |
| Magazine / Source | Biomolecular NMR Assignments |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.springerlink.com/content/3n38075w5h1l1082/ |
| Doi | http://dx.doi.org/10.1007/s12104-011-9293-6 |
| Field | Biochemistry |
| Keywords | protein; NMR assignment; PsbQ |
| Description | PsbQ is one of the extrinsic proteins situated on the lumenal surface of photosystem II (PSII) in the higher plants and green algae. Its three-dimensional structure was determined by X-ray crystallography with exception of the residues 14–33. To obtain further details about its structure and potentially its dynamics, we approached the problem by NMR. In this paper we report 1H, 15N, and 13C NMR assignments for the PsbQ protein. The very challenging oligo-proline stretches could be assigned using 13C-detected NMR experiments that enabled the assignments of twelve out of the thirteen proline residues of PsbQ. The identification of PsbQ secondary structure elements on the basis of our NMR data was accomplished with the programs TALOS+, web server CS23D and CS-Rosetta. |