Hydrogen/deuterium exchange mass spectrometry and its utilization

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F15%3A%230000659" target="_blank" >RIV/00209805:_____/15:#0000659 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.jri.2015.09.004" target="_blank" >http://dx.doi.org/10.1016/j.jri.2015.09.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jri.2015.09.004" target="_blank" >10.1016/j.jri.2015.09.004</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Hydrogen/deuterium exchange mass spectrometry and its utilization

Popis výsledku v původním jazyce

Hydrogen/deuterium exchange connected with mass spectrometry is increasingly applied for the interrogation of protein conformation, mapping protein dynamics, identification of protein-ligand interaction sites, and allosteric conformation changes. The dynamics of protein changes is determined with the m/z value of deuterated and non-deuterated protein or percentage of deuterium incorporation for the digested peptides. Hydrogen/deuterium exchange data are processed with selected software and finally quaternary structure of protein is visualized showing how different protein and ligand chains hook up with each other. Obtained results can help understand how protein interacts with its ligand and elucidate the role of this complex in a living organism. Utilization of this method is demonstrated by the amyloid-beta peptide aggregation associated with Alzheimer´s disease; determination of the structure toxin-co-regulated pili Vibrio cholerae in connection with its pathogenesis or revelation o

Název v anglickém jazyce

Hydrogen/deuterium exchange mass spectrometry and its utilization

Popis výsledku anglicky

Hydrogen/deuterium exchange connected with mass spectrometry is increasingly applied for the interrogation of protein conformation, mapping protein dynamics, identification of protein-ligand interaction sites, and allosteric conformation changes. The dynamics of protein changes is determined with the m/z value of deuterated and non-deuterated protein or percentage of deuterium incorporation for the digested peptides. Hydrogen/deuterium exchange data are processed with selected software and finally quaternary structure of protein is visualized showing how different protein and ligand chains hook up with each other. Obtained results can help understand how protein interacts with its ligand and elucidate the role of this complex in a living organism. Utilization of this method is demonstrated by the amyloid-beta peptide aggregation associated with Alzheimer´s disease; determination of the structure toxin-co-regulated pili Vibrio cholerae in connection with its pathogenesis or revelation o

Druh

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

CEP obor

EB - Genetika a molekulární biologie

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>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

Military medical science letters

ISSN

0165-0378

e-ISSN

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Svazek periodika

84

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

6

Strana od-do

146-151

Kód UT WoS článku

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EID výsledku v databázi Scopus

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