Backbone assignment and secondary structure of the PsbQ protein from Photosystem II

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F11%3A00052822" target="_blank" >RIV/00216224:14310/11:00052822 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/11:00372479 RIV/60076658:12640/11:43882310

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s12104-011-9293-6" target="_blank" >http://dx.doi.org/10.1007/s12104-011-9293-6</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s12104-011-9293-6" target="_blank" >10.1007/s12104-011-9293-6</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Backbone assignment and secondary structure of the PsbQ protein from Photosystem II

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Backbone assignment and secondary structure of the PsbQ protein from Photosystem II

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LC06010" target="_blank" >LC06010: Centrum biokatalýzy a biotransformací</a><br>

Návaznosti

R - Projekt Ramcoveho programu EK

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biomolecular NMR Assignments

ISSN

1874-2718

e-ISSN

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Svazek periodika

5

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

169-175

Kód UT WoS článku

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EID výsledku v databázi Scopus

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