Unique identification of proteins from small genome organisms: Theoretical feasibility of high throughput proteome analysis
Autor: | Ruth A. VanBogelen, Philip C. Andrews, James D. Cavalcoli, Brian Moldover |
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Rok vydání: | 1997 |
Předmět: |
Clinical Biochemistry
Reproducibility of Results Computational biology Hydrogen-Ion Concentration Biology Bioinformatics Biochemistry Genome Analytical Chemistry Isoelectric point Bacterial Proteins Stepping stone Proteome Escherichia coli Feasibility Studies Electrophoresis Gel Two-Dimensional Genomic information Identification (biology) Cluster analysis Throughput (business) Genome Bacterial |
Zdroj: | Electrophoresis. 18:2703-2708 |
ISSN: | 1522-2683 0173-0835 |
DOI: | 10.1002/elps.1150181503 |
Popis: | We evaluate current levels of accuracy for estimation of molecular weight (Mr) and isoelectric point (pI) to proteins on two-dimensional (2-D) gels as well as the distribution and clustering of proteins in the predicted proteome of E. coli. We also examine the ability to find single candidates within the predicted proteome for matching to a protein seen on 2-D gels, based on the current level of accuracy. We discuss the levels of accuracy needed to match predicted proteins to observed proteins based solely on Mr and pI criteria obtained from genomic information, and propose methodology to achieve this level of accuracy. In addition, we will address the future goals of this work since the small genomes of bacteria provide a foundation and stepping stone to similar studies in higher organisms. |
Databáze: | OpenAIRE |
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