Changes in Electrostatic Surface Potential of Na+/K+-ATPase Cytoplasmic Headpiece Induced by Cytoplasmic Ligand(s) Binding

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F09%3A00010189" target="_blank" >RIV/61989592:15310/09:00010189 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/09:00333696

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Changes in Electrostatic Surface Potential of Na+/K+-ATPase Cytoplasmic Headpiece Induced by Cytoplasmic Ligand(s) Binding

Popis výsledku v původním jazyce

Set of single-tryptophan mutants of the Na+/K+-ATPase isolated large cytoplasmic loop connecting transmembrane helices M4 and M5 (C45) was prepared to monitor effects of the natural cytoplasmic ligands (i.e. Mg2+ and/or ATP) binding. We introduced a novel method for the monitoring of the changes in the electrostatic surface potential (ESP) induced by ligand binding, using the quenching of the intrinsic tryptophan fluorescence by acrylamide or iodide. This approach opens new way to understanding the interactions within the proteins. Our experiments revealed that the C45 conformation in the presence of the ATP (without magnesium) substantially differed from the conformation in the presence of Mg2+ or MgATP or in the absence of any ligand not only in thesense of geometry but also in the sense of the ESP. Notably, the set of ?ESP-sensitive? residues was different from the set of ?geometry-sensitive? residues. Moreover, our data indicate that the effect of the ligand binding is not restric

Název v anglickém jazyce

Changes in Electrostatic Surface Potential of Na+/K+-ATPase Cytoplasmic Headpiece Induced by Cytoplasmic Ligand(s) Binding

Popis výsledku anglicky

Set of single-tryptophan mutants of the Na+/K+-ATPase isolated large cytoplasmic loop connecting transmembrane helices M4 and M5 (C45) was prepared to monitor effects of the natural cytoplasmic ligands (i.e. Mg2+ and/or ATP) binding. We introduced a novel method for the monitoring of the changes in the electrostatic surface potential (ESP) induced by ligand binding, using the quenching of the intrinsic tryptophan fluorescence by acrylamide or iodide. This approach opens new way to understanding the interactions within the proteins. Our experiments revealed that the C45 conformation in the presence of the ATP (without magnesium) substantially differed from the conformation in the presence of Mg2+ or MgATP or in the absence of any ligand not only in thesense of geometry but also in the sense of the ESP. Notably, the set of ?ESP-sensitive? residues was different from the set of ?geometry-sensitive? residues. Moreover, our data indicate that the effect of the ligand binding is not restric

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název periodika

Biophysical Journal

ISSN

0006-3495

e-ISSN

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Svazek periodika

97

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

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Kód UT WoS článku

000270380800027

EID výsledku v databázi Scopus

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