We have developed a computer program able to make user-customised databases derived from the public PIR non-redundant reference protein database. When the database of interest has been created, the user will generate the map of all the possible linear peptides containing one and two cysteines for each protein and combine them to calculate the mass of all the possible clusters of linear peptides linked by a disulphide bridge with a cysteine pair. It is also possible to create selected maps corresponding to peptides formed by the action of specific proteases. In this way, mass spectrometric data obtained from the hydrolysis of proteins of unknown sequence can be related to that contained in the database for quick disulphide assignment and protein identification. To confirm signal attribution, the program will also furnish the expected mass of cluster peptides after performing a cycle of Edman degradation. The utility of the program is discussed and examples of application are given. © 2005 Federation of European Biochemical Societies.
CysMap and CysJoin: Database and tools for protein disulphide localization / Caporale, C.; Bertini, L.; Pucci, Pietro; Buonocore, V.; Caruso, C.. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 579:14(2005), pp. 3048-3054. [10.1016/j.febslet.2005.04.061]
CysMap and CysJoin: Database and tools for protein disulphide localization
PUCCI, PIETRO;
2005
Abstract
We have developed a computer program able to make user-customised databases derived from the public PIR non-redundant reference protein database. When the database of interest has been created, the user will generate the map of all the possible linear peptides containing one and two cysteines for each protein and combine them to calculate the mass of all the possible clusters of linear peptides linked by a disulphide bridge with a cysteine pair. It is also possible to create selected maps corresponding to peptides formed by the action of specific proteases. In this way, mass spectrometric data obtained from the hydrolysis of proteins of unknown sequence can be related to that contained in the database for quick disulphide assignment and protein identification. To confirm signal attribution, the program will also furnish the expected mass of cluster peptides after performing a cycle of Edman degradation. The utility of the program is discussed and examples of application are given. © 2005 Federation of European Biochemical Societies.File | Dimensione | Formato | |
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