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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00012733%21RIV%2F2005%2FGA0%2F223305%2FN
rdf:type
n19:Vysledek skos:Concept
dcterms: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 identification 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 identification 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 identification
dcterms:title
Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry
skos:prefLabel
Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry
skos:notation
RIV/60461373:22330/04:00012733!RIV/2005/GA0/223305/N
n3:strany
1134-1138
n3:aktivita
n15:Z n15:P
n3:aktivity
P(GA203/02/0922), Z(MSM 223300006)
n3:cisloPeriodika
9
n3:dodaniDat
n12:2005
n3:domaciTvurceVysledku
n10:9046976 n10:6936903 n10:2194538 n10:1120530
n3:druhVysledku
n4:J
n3:duvernostUdaju
n8:S
n3:entitaPredkladatele
n6:predkladatel
n3:idSjednocenehoVysledku
554315
n3:idVysledku
RIV/60461373:22330/04:00012733
n3:jazykVysledku
n17:cze
n3:klicovaSlova
2-Hydroxy-5-nitrobenzyl bromide;Koshland's reagent;Protein surface mapping;Tryptophan modification;MALDI-TOF mass spectrometry;
n3:klicoveSlovo
n7:Tryptophan%20modification n7:MALDI-TOF%20mass%20spectrometry n7:2-Hydroxy-5-nitrobenzyl%20bromide n7:Protein%20surface%20mapping n7:Koshland%27s%20reagent
n3:kodStatuVydavatele
BE - Belgické království
n3:kontrolniKodProRIV
[4E14E274A4AB]
n3:nazevZdroje
Biochemical and Biophysical Research Communication
n3:obor
n11:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
4
n3:projekt
n18:GA203%2F02%2F0922
n3:rokUplatneniVysledku
n12:2004
n3:svazekPeriodika
323
n3:tvurceVysledku
Kodíček, Milan Hynek, Radovan Strohalm, Martin Šantrůček, Jiří
n3:zamer
n9:MSM%20223300006
s:issn
0006-291X
s:numberOfPages
5
n13:organizacniJednotka
22330