Dipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F17%3A00471291" target="_blank" >RIV/61388955:_____/17:00471291 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/anie.201611582" target="_blank" >http://dx.doi.org/10.1002/anie.201611582</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/anie.201611582" target="_blank" >10.1002/anie.201611582</a>
Alternative languages
Result language
angličtina
Original language name
Dipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure
Original language description
The active transport of ions across biological membranes requires their hydration shell to interact with the interior of membrane proteins. However, the influence of the external lipid phase on internal dielectric dynamics is hard to access by experiment. Using the octahelical transmembrane architecture of the copper-transporting P1B-type ATPase from Legionella pneumophila as a model structure, we have established the site-specific labeling of internal cysteines with a polarity-sensitive fluorophore. This enabled dipolar relaxation studies in a solubilized form of the protein and in its lipid-embedded state in nanodiscs. Time-dependent fluorescence shifts revealed the site-specific hydration and dipole mobility around the conserved ion-binding motif. The spatial distribution of both features is shaped significantly and independently of each other by membrane lateral pressure.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Angewandte Chemie - International Edition
ISSN
1433-7851
e-ISSN
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Volume of the periodical
56
Issue of the periodical within the volume
5
Country of publishing house
DE - GERMANY
Number of pages
4
Pages from-to
1269-1272
UT code for WoS article
000394997700014
EID of the result in the Scopus database
2-s2.0-85007324122