The modal distribution of protein isoelectric points reflects amino acid properties rather than sequence evolution

Two‐dimensional gel electrophoresis, a routine application in proteomics, separates proteins according to their molecular mass (Mr) and isoelectric point (pI). As the genomic sequences for more and more organisms are determined, the Mr and pI of all their proteins can be estimated computationally. T...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2004-04, Vol.4 (4), p.943-949
Main Authors: Weiller, Georg F., Caraux, Gilles, Sylvester, Nicole
Format: Article
Language:English
Subjects:
Algorithms
Amino Acids - chemistry
Analytical, structural and metabolic biochemistry
Bioinformatics
Biological and medical sciences
Computational Biology - methods
Computer Science
Databases, Protein
Electrophoresis, Gel, Two-Dimensional
Extremophiles
Fundamental and applied biological sciences. Psychology
Genome
Isoelectric Point
Miscellaneous
Multimodal distribution
Proteins
Proteins - chemistry
Statistics as Topic
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Summary:Two‐dimensional gel electrophoresis, a routine application in proteomics, separates proteins according to their molecular mass (Mr) and isoelectric point (pI). As the genomic sequences for more and more organisms are determined, the Mr and pI of all their proteins can be estimated computationally. The examination of several of these theoretical proteome plots has revealed a multimodal pI distribution, however, no conclusive explanation for this unusual distribution has so far been presented. We examined the pI distribution of 115 fully sequenced genomes and observed that the modal distribution does not reflect phylogeny or sequence evolution, but rather the chemical properties of amino acids. We provide a statistical explanation of why the observed distributions of pI values are multimodal.
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.200200648