ArticleProceedings of the National Academy of Sciences of the United States of America1993
Rapid identification of proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Teaching molecular genetics: Chapter 3--Proteomics in nephrology.Pediatric nephrology (Berlin, Germany) · 2006Review
- A statistical view of FMRFamide neuropeptide diversity.Molecular neurobiologyReview
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Authors and funding
1 author.
Funding
Abstract
The amino acid composition, molecular weight, and isoelectric point of a protein can all be easily and economically determined by current electrophoretic techniques. A method which uses such easily obtained data to identify proteins is described. A computer program first corrects for systematic errors in amino acid quantitation and then searches the current sequence database for proteins with amino acid compositions similar to the corrected values, taking into account the reliability of determination of each amino acid. The program also provides the calculated molecular weight, isoelectric point, and name of each candidate, providing three further independent criteria for protein identification. The program is surprisingly sensitive, and the composition data alone, if of good quality, usually suggest the correct protein as a strong candidate if it or a close homologue is present in the database. Further studies show that proteins in the current database have amino acid compositions distinct enough to allow this method to be generally applicable. The method is a quick and cost-effective first step in protein characterization and should become increasingly useful as the number of fully sequenced proteins continues to rise.
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