Mapping protein structural changes by quantitative cross-linking

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10294866" target="_blank" >RIV/00216208:11310/15:10294866 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00455585

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.ymeth.2015.05.027" target="_blank" >http://dx.doi.org/10.1016/j.ymeth.2015.05.027</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ymeth.2015.05.027" target="_blank" >10.1016/j.ymeth.2015.05.027</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mapping protein structural changes by quantitative cross-linking

Popis výsledku v původním jazyce

Chemical cross-linking is a promising technology for protein tertiary structure determination. Though the data has low spatial resolution, it is possible to obtain it at physiological conditions on proteins that are not amenable to standard high resolution techniques such as X-ray, NMR analysis and cryo-EM. Here we demonstrate the utilization of isotopically labeled chemical cross-linking to visualize protein conformation rearrangements. Since calmodulin exists in two distinct conformations (calcium-free and calcium-containing forms), we selected this protein for testing the potential and the limits of a new technique. After cross-linking of both calmodulin forms, the calcium-free and calcium-containing forms were mixed together and digested under different conditions and the products of proteolysis were monitored using high resolution mass spectrometry. Finally, the ratios of heavy/light cross-links were calculated by mMass open source platform.

Název v anglickém jazyce

Mapping protein structural changes by quantitative cross-linking

Popis výsledku anglicky

Chemical cross-linking is a promising technology for protein tertiary structure determination. Though the data has low spatial resolution, it is possible to obtain it at physiological conditions on proteins that are not amenable to standard high resolution techniques such as X-ray, NMR analysis and cryo-EM. Here we demonstrate the utilization of isotopically labeled chemical cross-linking to visualize protein conformation rearrangements. Since calmodulin exists in two distinct conformations (calcium-free and calcium-containing forms), we selected this protein for testing the potential and the limits of a new technique. After cross-linking of both calmodulin forms, the calcium-free and calcium-containing forms were mixed together and digested under different conditions and the products of proteolysis were monitored using high resolution mass spectrometry. Finally, the ratios of heavy/light cross-links were calculated by mMass open source platform.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Methods

ISSN

1046-2023

e-ISSN

—

Svazek periodika

89

Číslo periodika v rámci svazku

1 November 2015

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

112-120

Kód UT WoS článku

000365062800014

EID výsledku v databázi Scopus

2-s2.0-84946405388