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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00012917%21RIV%2F2005%2FGA0%2F223305%2FN
rdf:type
skos:Concept n17:Vysledek
dcterms:description
Amino acid residue-specific reactivity in proteins is of great current interest in structural biology as it provides information about solvent accessibility and reactivity of the residue and, consequently, about protein structure and possible interactions. In the work presented tyrosine residues of three model proteins with known spatial structure are modified with two tyrosine-specific reagents: tetranitromethane and iodine. Modified proteins were specifically digested by proteases and the mass of resulting peptide fragments was determined using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Our results show that there are only small differences in the extent of tyrosine residues modification by tetranitromethane and iodine. However, data dealing with accessibility of reactive residues obtained by chemical modifications are not completely identical with those obtained by nuclear magnetic resonance and X-ray crystallography. These interesting discrepancies can be caused Amino acid residue-specific reactivity in proteins is of great current interest in structural biology as it provides information about solvent accessibility and reactivity of the residue and, consequently, about protein structure and possible interactions. In the work presented tyrosine residues of three model proteins with known spatial structure are modified with two tyrosine-specific reagents: tetranitromethane and iodine. Modified proteins were specifically digested by proteases and the mass of resulting peptide fragments was determined using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Our results show that there are only small differences in the extent of tyrosine residues modification by tetranitromethane and iodine. However, data dealing with accessibility of reactive residues obtained by chemical modifications are not completely identical with those obtained by nuclear magnetic resonance and X-ray crystallography. These interesting discrepancies can be caused Amino acid residue-specific reactivity in proteins is of great current interest in structural biology as it provides information about solvent accessibility and reactivity of the residue and, consequently, about protein structure and possible interactions. In the work presented tyrosine residues of three model proteins with known spatial structure are modified with two tyrosine-specific reagents: tetranitromethane and iodine. Modified proteins were specifically digested by proteases and the mass of resulting peptide fragments was determined using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Our results show that there are only small differences in the extent of tyrosine residues modification by tetranitromethane and iodine. However, data dealing with accessibility of reactive residues obtained by chemical modifications are not completely identical with those obtained by nuclear magnetic resonance and X-ray crystallography. These interesting discrepancies can be caused
dcterms:title
Tyrosine residues modification studied by MALDI-TOF mass spectrometry Tyrosine residues modification studied by MALDI-TOF mass spectrometry Tyrosine residues modification studied by MALDI-TOF mass spectrometry
skos:prefLabel
Tyrosine residues modification studied by MALDI-TOF mass spectrometry Tyrosine residues modification studied by MALDI-TOF mass spectrometry Tyrosine residues modification studied by MALDI-TOF mass spectrometry
skos:notation
RIV/60461373:22330/04:00012917!RIV/2005/GA0/223305/N
n3:strany
1151-1156
n3:aktivita
n12:P n12:Z
n3:aktivity
P(GA203/02/0922), Z(MSM 223300006)
n3:cisloPeriodika
9
n3:dodaniDat
n15:2005
n3:domaciTvurceVysledku
n5:1120530 n5:9724486 n5:6936903 n5:2194538 n5:9046976
n3:druhVysledku
n4:J
n3:duvernostUdaju
n19:S
n3:entitaPredkladatele
n7:predkladatel
n3:idSjednocenehoVysledku
591122
n3:idVysledku
RIV/60461373:22330/04:00012917
n3:jazykVysledku
n13:cze
n3:klicovaSlova
MALDI-TOF mass spectrometry;Nitration;Iodination;Solvent accessibility;Surface mapping
n3:klicoveSlovo
n6:MALDI-TOF%20mass%20spectrometry n6:Solvent%20accessibility n6:Iodination n6:Surface%20mapping n6:Nitration
n3:kodStatuVydavatele
BE - Belgické království
n3:kontrolniKodProRIV
[1D0CDD034B66]
n3:nazevZdroje
Biochemical and Biophysical Research Communication
n3:obor
n18:CE
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
5
n3:projekt
n10:GA203%2F02%2F0922
n3:rokUplatneniVysledku
n15:2004
n3:svazekPeriodika
323
n3:tvurceVysledku
Strohalm, Martin Kadlčík, Vojtěch Kodíček, Milan Hynek, Radovan Šantrůček, Jiří
n3:zamer
n8:MSM%20223300006
s:issn
0006-291X
s:numberOfPages
6
n16:organizacniJednotka
22330