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Roughness of Transmembrane Helices Reduces Lipid Membrane Dynamics

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F18%3A00497636" target="_blank" >RIV/61388955:_____/18:00497636 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.isci.2018.11.026" target="_blank" >http://dx.doi.org/10.1016/j.isci.2018.11.026</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.isci.2018.11.026" target="_blank" >10.1016/j.isci.2018.11.026</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Roughness of Transmembrane Helices Reduces Lipid Membrane Dynamics

  • Original language description

    The dynamics of cellular membranes is primarily determined by lipid species forming a bilayer. Proteins are considered mainly as effector molecules of diverse cellular processes. In addition to large assemblies of proteins, which were found to influence properties of fluid membranes, biological membranes are densely populated by small, highly mobile proteins. However, little is known about the effect of such proteins on the dynamics of membranes. Using synthetic peptides, we demonstrate that transmembrane helices interfere with the mobility of membrane components by trapping lipid acyl chains on their rough surfaces. The effect is more pronounced in the presence of cholesterol, which segregates from the rough surface of helical peptides. This may contribute to the formation or stabilization of membrane heterogeneities. Since roughness is a general property of helical transmembrane segments, our results suggest that, independent of their size or cytoskeleton linkage, integral membrane proteins affect local membrane dynamics and organization.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    iScience

  • ISSN

    2589-0042

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    DEC 2018

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    11

  • Pages from-to

    87-97

  • UT code for WoS article

    000454331700008

  • EID of the result in the Scopus database