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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F20%3A00540021" target="_blank" >RIV/68378050:_____/20:00540021 - isvavai.cz</a>

Výsledek na webu

<a href="https://link.springer.com/protocol/10.1007%2F978-1-0716-0775-6_27" target="_blank" >https://link.springer.com/protocol/10.1007%2F978-1-0716-0775-6_27</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/978-1-0716-0775-6_27" target="_blank" >10.1007/978-1-0716-0775-6_27</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

Microtubules, polymers of the heterodimeric protein αβ-tubulin, are indispensable for many cellularnactivities such as maintenance of cell shape, division, migration, and ordered vesicle transport. In vitronassays to study microtubule functions and their regulation by associated proteins require the availability of assembly-competent purified tubulin. However, tubulin is a thermolabile protein that rapidly converts into a nonpolymerizing state. For this reason, it is usually stored at -80 C or liquid nitrogen 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 the evaluation of tubulin functions in rehydrated samples.n

Název v anglickém jazyce

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

Popis výsledku anglicky

Microtubules, polymers of the heterodimeric protein αβ-tubulin, are indispensable for many cellularnactivities such as maintenance of cell shape, division, migration, and ordered vesicle transport. In vitronassays to study microtubule functions and their regulation by associated proteins require the availability of assembly-competent purified tubulin. However, tubulin is a thermolabile protein that rapidly converts into a nonpolymerizing state. For this reason, it is usually stored at -80 C or liquid nitrogen 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 the evaluation of tubulin functions in rehydrated samples.n

Druh

C - Kapitola v odborné knize

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

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

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název knihy nebo sborníku

Protein downstream processing: Design, Development And Application of High and Low-Resolution Methods (N. Labrou Ed.) 2nd edition

ISBN

978-1-0716-0775-6

Počet stran výsledku

19

Strana od-do

417-435

Počet stran knihy

511

Název nakladatele

Humana Press

Místo vydání

New York

Kód UT WoS kapitoly

000697782600028