Mass spectrometry: Difference between revisions
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Mass Spectrometry in the process in where proteins can be identified. Whether it be a single [[Protein|protein]], or a collections of [[Proteins|proteins]], obatined after procedures such as [[Gel electrophoresis|gel electrophoresis]] or by [[Column chromatography|column chromatography]].The proteins in the sample are firstly broken down into smaller peptides, where they are ionized creating a postive charge. These ionized peptides are accelerated via an electric field towards a decetor. The mass to charge ratio of these ions affect the time it takes for them to reach the dector, large peptides moving slower and higher charged molecules move faster.<ref>Alberts et al (2008) Molecular Biology Of The Cell, 5th Edition</ref> The masses of the peptides obtained by the detector can then be measured and compared to other well known peptides in a database, determing the genomic seqeunce and ultimately the [[Protein|protein]]. | |||
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=== References === | === References === | ||
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Latest revision as of 01:15, 28 November 2014
Mass Spectrometry in the process in where proteins can be identified. Whether it be a single protein, or a collections of proteins, obatined after procedures such as gel electrophoresis or by column chromatography.The proteins in the sample are firstly broken down into smaller peptides, where they are ionized creating a postive charge. These ionized peptides are accelerated via an electric field towards a decetor. The mass to charge ratio of these ions affect the time it takes for them to reach the dector, large peptides moving slower and higher charged molecules move faster.[1] The masses of the peptides obtained by the detector can then be measured and compared to other well known peptides in a database, determing the genomic seqeunce and ultimately the protein.
References
- ↑ Alberts et al (2008) Molecular Biology Of The Cell, 5th Edition