Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.

Mass spectrometry (MS) techniques have, over the last twenty years, found their stable place in the structural biology toolkit. They are not only employed to provide information on the protein primary sequence, but are increasingly used to probe higher orders of protein structure as well. They may n...

Full description

Bibliographic Details
Main Author: Kádek, Alan
Other Authors: Man, Petr
Format: Doctoral Thesis
Language:English
Published: 2016
Online Access:http://www.nusl.cz/ntk/nusl-353405
id ndltd-nusl.cz-oai-invenio.nusl.cz-353405
record_format oai_dc
spelling ndltd-nusl.cz-oai-invenio.nusl.cz-3534052019-05-18T03:26:16Z Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie. Study of conformations and conformational changes of proteins using mass spectrometric methods. Kádek, Alan Man, Petr Šebela, Marek Hnízda, Aleš Mass spectrometry (MS) techniques have, over the last twenty years, found their stable place in the structural biology toolkit. They are not only employed to provide information on the protein primary sequence, but are increasingly used to probe higher orders of protein structure as well. They may not boast the atomic resolution and the ability to directly provide structural coordinates, but on the other hand suffer from very few experimental limitations as they are able to work under native conditions in solution, provide data fast, with low sample consumption and for proteins and complexes of vastly differing sizes. Perhaps most importantly, they may often be employed to study conformational dynamics of proteins and can thus complement other methods with higher spatial resolution in integrative structural biology approaches. The main focus of this Ph.D. thesis was hydrogen / deuterium exchange coupled to MS (HXMS), which is one of the most widespread structural MS methods. Recombinantly produced aspartic protease nepenthesin-1 from Nepenthes pitcher plants was characterized, immobilized and extensively tested with the intention to expand the portfolio of aspartic proteases in HXMS workflow and to improve the spatial resolution of the technique. Following successful implementation of nepenthesin-1... 2016 info:eu-repo/semantics/doctoralThesis http://www.nusl.cz/ntk/nusl-353405 eng info:eu-repo/semantics/restrictedAccess
collection NDLTD
language English
format Doctoral Thesis
sources NDLTD
description Mass spectrometry (MS) techniques have, over the last twenty years, found their stable place in the structural biology toolkit. They are not only employed to provide information on the protein primary sequence, but are increasingly used to probe higher orders of protein structure as well. They may not boast the atomic resolution and the ability to directly provide structural coordinates, but on the other hand suffer from very few experimental limitations as they are able to work under native conditions in solution, provide data fast, with low sample consumption and for proteins and complexes of vastly differing sizes. Perhaps most importantly, they may often be employed to study conformational dynamics of proteins and can thus complement other methods with higher spatial resolution in integrative structural biology approaches. The main focus of this Ph.D. thesis was hydrogen / deuterium exchange coupled to MS (HXMS), which is one of the most widespread structural MS methods. Recombinantly produced aspartic protease nepenthesin-1 from Nepenthes pitcher plants was characterized, immobilized and extensively tested with the intention to expand the portfolio of aspartic proteases in HXMS workflow and to improve the spatial resolution of the technique. Following successful implementation of nepenthesin-1...
author2 Man, Petr
author_facet Man, Petr
Kádek, Alan
author Kádek, Alan
spellingShingle Kádek, Alan
Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
author_sort Kádek, Alan
title Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
title_short Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
title_full Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
title_fullStr Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
title_full_unstemmed Studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
title_sort studium konformací a konformačních změn proteinů metodami hmotnostní spektrometrie.
publishDate 2016
url http://www.nusl.cz/ntk/nusl-353405
work_keys_str_mv AT kadekalan studiumkonformaciakonformacnichzmenproteinumetodamihmotnostnispektrometrie
AT kadekalan studyofconformationsandconformationalchangesofproteinsusingmassspectrometricmethods
_version_ 1719190950614401024