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| rdf:type
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| 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 (en)
- 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 (cs)
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| 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 (en)
- Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry (cs)
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| 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 (en)
- Analysis of tryptophan surface accessibility in proteins by MALDI-TOF mass spectrometry (cs)
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| skos:notation
| - RIV/60461373:22330/04:00012733!RIV/2005/GA0/223305/N
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
| - P(GA203/02/0922), Z(MSM 223300006)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
| |
| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/60461373:22330/04:00012733
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - 2-Hydroxy-5-nitrobenzyl bromide;Koshland's reagent;Protein surface mapping;Tryptophan modification;MALDI-TOF mass spectrometry; (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Biochemical and Biophysical Research Communication
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
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| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Hynek, Radovan
- Kodíček, Milan
- Šantrůček, Jiří
- Strohalm, Martin
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| http://linked.open...n/vavai/riv/zamer
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| issn
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| number of pages
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| http://localhost/t...ganizacniJednotka
| |
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