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Stabilization of protein by freeze-drying in the presence of trehalose: a case study of tubulin

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F14%3A00434353" target="_blank" >RIV/68378050:_____/14:00434353 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1007/978-1-62703-977-2_32" target="_blank" >http://dx.doi.org/10.1007/978-1-62703-977-2_32</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/978-1-62703-977-2_32" target="_blank" >10.1007/978-1-62703-977-2_32</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Stabilization of protein by freeze-drying in the presence of trehalose: a case study of tubulin

  • Original language description

    Microtubules, polymers of the heterodimeric protein ??-tubulin, are indispensable for many cellular activities such as maintenance of cell shape, division, migration, and ordered vesicle transport. In vitro assays to study microtubule functions and theirregulation by associated proteins require the availability of assembly-competent purified tubulin. However, tubulin is a thermolabile protein that rapidly converts into non-polymerizing state. For this reason it is usually stored at 80 °C to preserve its conformation and polymerization properties. In this chapter we describe a method for freeze-drying of assembly-competent tubulin in the presence of nonreducing sugar trehalose and methods enabling evaluation of tubulin functions in rehydrated samples.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2014

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Methods in Molecular Biology

  • ISSN

    1064-3745

  • e-ISSN

  • Volume of the periodical

    1129

  • Issue of the periodical within the volume

    February

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    16

  • Pages from-to

    443-458

  • UT code for WoS article

    000337104300033

  • EID of the result in the Scopus database