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

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

čeština

Original language name

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

Original language description

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

Czech name

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

Czech description

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

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/GA203%2F02%2F0922" target="_blank" >GA203/02/0922: Application of MALDI-TOF (matrix assisted laser desorption ionisation - Time of Flight) mass spectrometry on the determination of protein conformation</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2004

Confidentiality

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

Name of the periodical

Biochemical and Biophysical Research Communication

ISSN

0006-291X

e-ISSN

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Volume of the periodical

323

Issue of the periodical within the volume

9

Country of publishing house

BE - BELGIUM

Number of pages

5

Pages from-to

1134-1138

UT code for WoS article

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EID of the result in the Scopus database

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