Study of Protein Conformational Dynamics Using Hydrogen/Deuterium Exchange Mass Spectrometry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F23%3A00079274" target="_blank" >RIV/00209805:_____/23:00079274 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/23:00133541

Výsledek na webu

<a href="https://pubmed.ncbi.nlm.nih.gov/37093484/" target="_blank" >https://pubmed.ncbi.nlm.nih.gov/37093484/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/978-1-0716-3147-8_18" target="_blank" >10.1007/978-1-0716-3147-8_18</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Study of Protein Conformational Dynamics Using Hydrogen/Deuterium Exchange Mass Spectrometry

Popis výsledku v původním jazyce

Intrinsic protein dynamics contribute to their biological functions. Rational engineering of protein dynamics is extremely challenging with only a handful of successful examples. Hydrogen/deuterium exchange coupled to mass spectrometry (HDX-MS) represents a powerful technique for quantitative analysis of protein dynamics. Here we provide a detailed description of the preparation of protein samples, collection of high-quality data, and their in-depth analysis using various computational tools. We illustrate the application of HDX-MS for the study of protein dynamics in the rational engineering of flexible loops in the reconstructed ancestor of haloalkane dehalogenase and Renilla luciferase. These experiments provided unique and valuable data rigorously describing the modification of protein dynamics upon grafting of the loop-helix element. Tips and tricks are provided to stimulate the wider use of HDX-MS to study and engineer protein dynamics. (C) 2023, The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Název v anglickém jazyce

Study of Protein Conformational Dynamics Using Hydrogen/Deuterium Exchange Mass Spectrometry

Popis výsledku anglicky

Intrinsic protein dynamics contribute to their biological functions. Rational engineering of protein dynamics is extremely challenging with only a handful of successful examples. Hydrogen/deuterium exchange coupled to mass spectrometry (HDX-MS) represents a powerful technique for quantitative analysis of protein dynamics. Here we provide a detailed description of the preparation of protein samples, collection of high-quality data, and their in-depth analysis using various computational tools. We illustrate the application of HDX-MS for the study of protein dynamics in the rational engineering of flexible loops in the reconstructed ancestor of haloalkane dehalogenase and Renilla luciferase. These experiments provided unique and valuable data rigorously describing the modification of protein dynamics upon grafting of the loop-helix element. Tips and tricks are provided to stimulate the wider use of HDX-MS to study and engineer protein dynamics. (C) 2023, The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Druh

C - Kapitola v odborné knize

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

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

2023

Kód důvěrnosti údajů

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

Název knihy nebo sborníku

Advanced Methods in Structural Biology

ISBN

978-1-07-163146-1

Počet stran výsledku

26

Strana od-do

1-26

Počet stran knihy

462

Název nakladatele

Humana Press

Místo vydání

Totowa

Kód UT WoS kapitoly

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