"Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica" . "4"^^ . "Olomouc" . . . "RIV/60461373:22330/04:00012916" . "Tyrosine residues modification studied by maldi-tof mass spectrometry"@en . . "tyrosine;surface accessibility;MALDI-TOF MS"@en . "4"^^ . "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" . "1"^^ . . . . "591121" . "33" . "Tyrosine residues modification studied by maldi-tof mass spectrometry" . "2004-08-31+02:00"^^ . "22330" . "Studium modifikac\u00ED tyrosinov\u00FDch zbytk\u016F pomoc\u00ED MALDI-TOF MS"@cs . "Olomouc, Czech Republic" . . . "Kod\u00ED\u010Dek, Milan" . . "\u0160antr\u016F\u010Dek, Ji\u0159\u00ED" . "Hynek, Radovan" . . . "Studium modifikac\u00ED tyrosinov\u00FDch zbytk\u016F pomoc\u00ED 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"@en . "Univerzita Palack\u00E9ho v Olomouci" . "[9145594C31CB]" . . "Tyrosine residues modification studied by maldi-tof mass spectrometry"@en . "RIV/60461373:22330/04:00012916!RIV/2005/GA0/223305/N" . "P(GA203/02/0922), Z(MSM 223300006)" . . "80-244-0882-1" . "Tyrosine residues modification studied by maldi-tof mass spectrometry" . . . "Strohalm, Martin" . "Studium modifikac\u00ED tyrosinov\u00FDch zbytk\u016F pomoc\u00ED MALDI-TOF MS"@cs . . .