Tyrosine residues modification studied by MALDI-TOF mass spectrometry

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2004-10, Vol.323 (4), p.1151-1156
Main Authors: Šantrůček, Jiří, Strohalm, Martin, Kadlčík, Vojtěch, Hynek, Radovan, Kodíček, Milan
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Animals
Binding Sites
Computer Simulation
Cytochromes c - chemistry
Humans
Iodination
Iodine - chemistry
MALDI-TOF mass spectrometry
Models, Molecular
Muramidase - chemistry
Nitration
Protein Binding
Protein Conformation
Proteins - chemistry
Serum Albumin - chemistry
Solvent accessibility
Solvents - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Surface mapping
Tetranitromethane - chemistry
Tyrosine - chemistry
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Summary: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 by local molecular dynamics and/or by specific chemical structure of the residues surrounding.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.08.214