Analysa povrchové dostupnosti tryptofanů pomocí hmotnostní spektrometrie MALDI-TOF

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012732" target="_blank" >RIV/60461373:22330/04:00012732 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Analysis of tryptophan surface accessibility by MALDI-TOF mass spectrometry

Popis výsledku v původním jazyce

Side chains of surface accessible amino acids play very important role in a biological activities of proteins. They can act as a part of enzyme's active center or participate on many intermolecular interactions. Information about the surface accessibility of selected amino acids can contribute to understanding the protein structure and function. The main interest of this work is to find out whether a specific chemical modification of tryptophan side chain in a molecule of a native protein could reflectssome relevant information about the accessibility and subsequently, information about the protein conformation. The reaction with 2-hydroxy-5-nitrobenzyl bromide (HNB) as a common and highly specific covalent modification of tryptophan seems to be veryuseful for this purposes.This method is based on the side chain modification followed by the analysis of the tryptic digest by MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass spectrometry. The procedure was tes

Název v anglickém jazyce

Analysis of tryptophan surface accessibility by MALDI-TOF mass spectrometry

Popis výsledku anglicky

Side chains of surface accessible amino acids play very important role in a biological activities of proteins. They can act as a part of enzyme's active center or participate on many intermolecular interactions. Information about the surface accessibility of selected amino acids can contribute to understanding the protein structure and function. The main interest of this work is to find out whether a specific chemical modification of tryptophan side chain in a molecule of a native protein could reflectssome relevant information about the accessibility and subsequently, information about the protein conformation. The reaction with 2-hydroxy-5-nitrobenzyl bromide (HNB) as a common and highly specific covalent modification of tryptophan seems to be veryuseful for this purposes.This method is based on the side chain modification followed by the analysis of the tryptic digest by MALDI-TOF (matrix-assisted laser desorption/ionization time-of-flight) mass spectrometry. The procedure was tes

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Studium konformace bílkovin pomocí hmotnostní spektrometrie na principu MALDI-TOF (Matrix Assisted Laser Desorption Ionisation - Time Of Flight)</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISBN

80-2440882-1

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

34

Název nakladatele

Univerzita Palackého

Místo vydání

Olomouc

Místo konání akce

Olomouc, Czech Republic

Datum konání akce

31. 8. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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