The Application of an Emerging Technique for Protein-Protein Interaction Interface Mapping: The Combination of Photo-Initiated Cross-Linking Protein Nanoprobes with Mass Spectrometry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10283840" target="_blank" >RIV/00216208:11310/14:10283840 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/14:00440657

Výsledek na webu

<a href="http://dx.doi.org/10.3390/ijms15069224" target="_blank" >http://dx.doi.org/10.3390/ijms15069224</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/ijms15069224" target="_blank" >10.3390/ijms15069224</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The Application of an Emerging Technique for Protein-Protein Interaction Interface Mapping: The Combination of Photo-Initiated Cross-Linking Protein Nanoprobes with Mass Spectrometry

Popis výsledku v původním jazyce

Protein-protein interaction was investigated using a protein nanoprobe capable of photo-initiated cross-linking in combination with high-resolution and tandem mass spectrometry. This emerging experimental approach introduces photo-analogs of amino acidswithin a protein sequence during its recombinant expression, preserves native protein structure and is suitable for mapping the contact between two proteins. The contact surface regions involved in the well-characterized interaction between two moleculesof human 14-3-3 zeta regulatory protein were used as a model. The employed photo-initiated cross-linking techniques extend the number of residues shown to be within interaction distance in the contact surface of the 14-3-3 lambda dimer (Gln8-Met78). Theresults of this study are in agreement with our previously published data from molecular dynamic calculations based on high-resolution chemical cross-linking data and Hydrogen/Deuterium exchange mass spectrometry. The observed contact is

Název v anglickém jazyce

The Application of an Emerging Technique for Protein-Protein Interaction Interface Mapping: The Combination of Photo-Initiated Cross-Linking Protein Nanoprobes with Mass Spectrometry

Popis výsledku anglicky

Protein-protein interaction was investigated using a protein nanoprobe capable of photo-initiated cross-linking in combination with high-resolution and tandem mass spectrometry. This emerging experimental approach introduces photo-analogs of amino acidswithin a protein sequence during its recombinant expression, preserves native protein structure and is suitable for mapping the contact between two proteins. The contact surface regions involved in the well-characterized interaction between two moleculesof human 14-3-3 zeta regulatory protein were used as a model. The employed photo-initiated cross-linking techniques extend the number of residues shown to be within interaction distance in the contact surface of the 14-3-3 lambda dimer (Gln8-Met78). Theresults of this study are in agreement with our previously published data from molecular dynamic calculations based on high-resolution chemical cross-linking data and Hydrogen/Deuterium exchange mass spectrometry. The observed contact is

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP207%2F12%2F0627" target="_blank" >GAP207/12/0627: INTERAKCE SAVČÍHO MIKROSOMÁLNÍHO CYTOCHROMU P450 S REDOX PARTNERY - TOPOLOGIE A STRUKTURNĚ-FUNKČNÍ VZTAHY</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

International Journal of Molecular Sciences

ISSN

1422-0067

e-ISSN

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Svazek periodika

15

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

18

Strana od-do

9224-9241

Kód UT WoS článku

000338639000004

EID výsledku v databázi Scopus

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