| HORNIČÁKOVÁ, Michaela, Jaroslava KOHOUTOVÁ, Judith SCHLAGNITWEIT, Christian WOLFSCHLAGER, Rudiger ETTRICH, Radovan FIALA, Wolfgang SCHOEFBERGER and Norbert MÜLLER. Backbone assignment and secondary structure of the PsbQ protein from Photosystem II. Biomolecular NMR Assignments. DORDRECHT: SPRINGER, 2011, vol. 5, No 2, p. 169-175. ISSN 1874-2718. Available from: https://dx.doi.org/10.1007/s12104-011-9293-6. |
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@article{947152,
author = {Horničáková, Michaela and Kohoutová, Jaroslava and Schlagnitweit, Judith and Wolfschlager, Christian and Ettrich, Rudiger and Fiala, Radovan and Schoefberger, Wolfgang and Müller, Norbert},
article_location = {DORDRECHT},
article_number = {2},
doi = {http://dx.doi.org/10.1007/s12104-011-9293-6},
keywords = {protein; NMR assignment; PsbQ},
language = {eng},
issn = {1874-2718},
journal = {Biomolecular NMR Assignments},
title = {Backbone assignment and secondary structure of the PsbQ protein from Photosystem II},
url = {http://www.springerlink.com/content/3n38075w5h1l1082/},
volume = {5},
year = {2011}
}
TY - JOUR
ID - 947152
AU - Horničáková, Michaela - Kohoutová, Jaroslava - Schlagnitweit, Judith - Wolfschlager, Christian - Ettrich, Rudiger - Fiala, Radovan - Schoefberger, Wolfgang - Müller, Norbert
PY - 2011
TI - Backbone assignment and secondary structure of the PsbQ protein from Photosystem II
JF - Biomolecular NMR Assignments
VL - 5
IS - 2
SP - 169-175
EP - 169-175
PB - SPRINGER
SN - 18742718
KW - protein
KW - NMR assignment
KW - PsbQ
UR - http://www.springerlink.com/content/3n38075w5h1l1082/
N2 - 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.
ER -
HORNIČÁKOVÁ, Michaela, Jaroslava KOHOUTOVÁ, Judith SCHLAGNITWEIT, Christian WOLFSCHLAGER, Rudiger ETTRICH, Radovan FIALA, Wolfgang SCHOEFBERGER and Norbert MÜLLER. Backbone assignment and secondary structure of the PsbQ protein from Photosystem II. \textit{Biomolecular NMR Assignments}. DORDRECHT: SPRINGER, 2011, vol.~5, No~2, p.~169-175. ISSN~1874-2718. Available from: https://dx.doi.org/10.1007/s12104-011-9293-6.
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