About: Tyrosine residues modification studied by maldi-tof mass spectrometry

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Studium modifikací tyrosinových zbytků pomocí MALDI-TOF MS (cs) Residue specific reactivity is of great current interest in structural biology as it provides information about the solvent accessibility and/or reactivity of a residue that can be used to probe protein structure and interactions. Although NMR and X-ray crystallography can give very detailed information about the solvent accesibility and environment of a specific residue, both methods are time-consuming and require miligrams of proteins. The development of mass spectrometry in protein science provides a sensitive and quick methodology for the measurement of molecular weights of peptide fragments, which allows one to identify the modified sites in the protein using micrograms of protein.In presented work tyrosine residues of three model proteins with known spatial structure (horse heart cytochrome c, chicken egg white lysozyme and human serum albumin) were modified with two reagents specific for tyrosine: tetranitromethane and iodine. Modified proteins were specifically digested with proteases and mass Residue specific reactivity is of great current interest in structural biology as it provides information about the solvent accessibility and/or reactivity of a residue that can be used to probe protein structure and interactions. Although NMR and X-ray crystallography can give very detailed information about the solvent accesibility and environment of a specific residue, both methods are time-consuming and require miligrams of proteins. The development of mass spectrometry in protein science provides a sensitive and quick methodology for the measurement of molecular weights of peptide fragments, which allows one to identify the modified sites in the protein using micrograms of protein.In presented work tyrosine residues of three model proteins with known spatial structure (horse heart cytochrome c, chicken egg white lysozyme and human serum albumin) were modified with two reagents specific for tyrosine: tetranitromethane and iodine. Modified proteins were specifically digested with proteases and mass (en)
Title	Studium modifikací tyrosinových zbytků pomocí MALDI-TOF MS (cs) Tyrosine residues modification studied by maldi-tof mass spectrometry Tyrosine residues modification studied by maldi-tof mass spectrometry (en)
skos:prefLabel	Studium modifikací tyrosinových zbytků pomocí MALDI-TOF MS (cs) Tyrosine residues modification studied by maldi-tof mass spectrometry Tyrosine residues modification studied by maldi-tof mass spectrometry (en)
skos:notation	RIV/60461373:22330/04:00012916!RIV/2005/GA0/223305/N
http://linked.open.../vavai/riv/strany	33
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA203/02/0922), Z(MSM 223300006)
http://linked.open...vai/riv/dodaniDat	2005
http://linked.open...aciTvurceVysledku	Šantrůček, Jiří Hynek, Radovan Kodíček, Milan Strohalm, Martin
http://linked.open.../riv/druhVysledku	D - Článek ve sborníku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Vysoká škola chemicko-technologická v Praze / Fakulta potravinářské a biochemické technologie
http://linked.open...dnocenehoVysledku	591121
http://linked.open...ai/riv/idVysledku	RIV/60461373:22330/04:00012916
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	tyrosine;surface accessibility;MALDI-TOF MS (en)
http://linked.open.../riv/klicoveSlovo	surface accessibility tyrosine MALDI-TOF MS
http://linked.open...ontrolniKodProRIV	[9145594C31CB]
http://linked.open...v/mistoKonaniAkce	Olomouc, Czech Republic
http://linked.open...i/riv/mistoVydani	Olomouc
http://linked.open...i/riv/nazevZdroje	Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	Application of MALDI-TOF (matrix assisted laser desorption ionisation - Time of Flight) mass spectrometry on the determination of protein conformation
http://linked.open...UplatneniVysledku	2004
http://linked.open...iv/tvurceVysledku	Hynek, Radovan Kodíček, Milan Šantrůček, Jiří Strohalm, Martin
http://linked.open...vavai/riv/typAkce	WRD - Světová
http://linked.open.../riv/zahajeniAkce	2004-08-31 (xsd:date)
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20223300006
number of pages	1 (xsd:int)
http://purl.org/ne...btex#hasPublisher	Univerzita Palackého v Olomouci
https://schema.org/isbn	80-244-0882-1
http://localhost/t...ganizacniJednotka	22330

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