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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/67985823:_____/09:00333696

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    BO - Biophysics

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

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

Others

  • Publication year

    2009

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biophysical Journal

  • ISSN

    0006-3495

  • e-ISSN

  • Volume of the periodical

    97

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

  • UT code for WoS article

    000270380800027

  • EID of the result in the Scopus database