Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012733" target="_blank" >RIV/60461373:22330/04:00012733 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

čeština

Název v původním jazyce

Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry

Popis výsledku v původním jazyce

Surface accessible amino acids can play an important role in proteins. They can participate in enzyme s active center structure or in specific intermolecular interactions. Thus, the information about selected amino acids surface accessibility can contribute to the understanding of protein structure and function. In this paper, we present a simple method for surface accessibility mapping of tryptophan side chains by their chemical modification and identification by MALDI-TOF mass spectrometry. The reaction with 2-hydroxy-5-nitrobenzyl bromide, a common and highly specific covalent modification of tryptophan, seems to be very useful for this purpose. The method was tested on four model proteins with known spatial structure. In the native proteins (1) only surface accessible tryptophan side chains were found to react with the modification agent and (2) no buried one was found to react at lower reagent concentrations. These results indicate that the described ethod can be a potent tool for

Název v anglickém jazyce

Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry

Popis výsledku anglicky

Surface accessible amino acids can play an important role in proteins. They can participate in enzyme s active center structure or in specific intermolecular interactions. Thus, the information about selected amino acids surface accessibility can contribute to the understanding of protein structure and function. In this paper, we present a simple method for surface accessibility mapping of tryptophan side chains by their chemical modification and identification by MALDI-TOF mass spectrometry. The reaction with 2-hydroxy-5-nitrobenzyl bromide, a common and highly specific covalent modification of tryptophan, seems to be very useful for this purpose. The method was tested on four model proteins with known spatial structure. In the native proteins (1) only surface accessible tryptophan side chains were found to react with the modification agent and (2) no buried one was found to react at lower reagent concentrations. These results indicate that the described ethod can be a potent tool for

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/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 periodika

Biochemical and Biophysical Research Communication

ISSN

0006-291X

e-ISSN

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Svazek periodika

323

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

5

Strana od-do

1134-1138

Kód UT WoS článku

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EID výsledku v databázi Scopus

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