"32" . "Is It Possible to Study Conformation of an Unpurified Protein?"@en . "569022" . "4"^^ . . "Univerzita Palack\u00E9ho v Olomouci" . . "Olomouc" . "Je mo\u017En\u00E9 studovat konformace %22ne\u010Dist\u00FDch%22 protein\u016F?"@cs . . . . . . . . "Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica" . "Hynek, Radovan" . "\u0160antr\u016F\u010Dek, Ji\u0159\u00ED" . "Is It Possible to Study Conformation of an Unpurified Protein?" . "Je mo\u017En\u00E9 studovat konformace %22ne\u010Dist\u00FDch%22 protein\u016F?"@cs . . . . "Kod\u00ED\u010Dek, Milan" . . "22330" . . "2004-08-31+02:00"^^ . "P(GA203/02/0922), Z(MSM 223300006)" . "Olomouc, Czech Republic" . "Is It Possible to Study Conformation of an Unpurified Protein?"@en . . . "During the last period enormous progress in protein conformation studies has been made thanks to the methods of X-ray crystalography as well as of NMR spectroscopy. These two methods are able to provide information about localization of individual atoms in three-dimensional structure of the protein. In addition to these %22absolute%22 methods, different quicker, cheaper and technically less demanding methods (circular dichroism, fluorimetry etc.) are available; they usually give sensitive information about changes in protein conformation and facilitate to compare structures of functionally analogical proteins.Chemical modifications of proteins have already been successfully performed in order to obtain information about localization of certain amino acid residues in protein globule [1,2]. These methods work on a simple principle: 1) To a native protein of known covalent structure a specific agent, which modifies a single (or limited number) amino acid side chain, is added. 2) The excess of the" . "80-244-0882-1" . . "[272B00757BF9]" . "RIV/60461373:22330/04:00012822" . . "RIV/60461373:22330/04:00012822!RIV/2005/GA0/223305/N" . "Strohalm, Martin" . "Je mo\u017En\u00E9 studovat konformace %22ne\u010Dist\u00FDch%22 protein\u016F?"@cs . . "tryptophan;tyrosine;surface accessibility;MALDI-TOF MS"@en . "During the last period enormous progress in protein conformation studies has been made thanks to the methods of X-ray crystalography as well as of NMR spectroscopy. These two methods are able to provide information about localization of individual atoms in three-dimensional structure of the protein. In addition to these %22absolute%22 methods, different quicker, cheaper and technically less demanding methods (circular dichroism, fluorimetry etc.) are available; they usually give sensitive information about changes in protein conformation and facilitate to compare structures of functionally analogical proteins.Chemical modifications of proteins have already been successfully performed in order to obtain information about localization of certain amino acid residues in protein globule [1,2]. These methods work on a simple principle: 1) To a native protein of known covalent structure a specific agent, which modifies a single (or limited number) amino acid side chain, is added. 2) The excess of the"@en . "1"^^ . "4"^^ . "Is It Possible to Study Conformation of an Unpurified Protein?" . . . .