BMC Genomics

official impact factor 4.21

Open Access Research article

An evolutionary and structural characterization of mammalian protein complex organization

Philip Wong1, Sonja Althammer1, Andrea Hildebrand1, Andreas Kirschner2, Philipp Pagel1,2, Bernd Geissler2, Pawel Smialowski1,2, Florian Blöchl1, Matthias Oesterheld1, Thorsten Schmidt1,2, Normann Strack1, Fabian J Theis1,3, Andreas Ruepp1 and Dmitrij Frishman1,2*

Author Affiliations

1 Helmholtz Center Munich – German Research Center for Environmental Health (GmbH), Institute of Bioinformatics and Systems Biology, Ingolstädter Landstraße 1 D-85764 Neuherberg, Germany

2 Department of Genome Oriented Bioinformatics, Technische Universität München, Wissenschaftzentrum Weihenstephan, 85350 Freising, Germany

3 Max-Planck-Institute for Dynamics and Self-Organization, Bunsenstrasse 10, 37073 Göttingen, Germany

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BMC Genomics 2008, 9:629 doi:10.1186/1471-2164-9-629

Published: 23 December 2008

Additional files

Additional File 1:

Description of the protein complex data. A detailed description of annotated and random complex data used.

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Additional File 2:

Benchmark of PSIPRED. A benchmark of PSIPRED's ability to predict secondary structure content from protein sequences is provided.

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Additional File 3:

Yeast complex complexity and participation distributions. The distribution of yeast complex complexity and participation approximately follows a power- law.

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Additional File 4:

Mammalian complex complexity and protein length. The mean length of proteins in available mammalian complexes is examined with respect to complex complexity.

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Additional File 5:

Median length of proteins in annotated human complexes. The median length of proteins in human complexes is examined with respect to complex complexity.

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Additional File 6:

Yeast complex complexity and protein length. The mean length of proteins in available yeast complexes is examined with respect to complex complexity.

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Additional File 7:

Length distribution of human mitochondrial proteins. The length distribution of human mitochondrial proteins is plotted.

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Additional File 8:

Random complexes and dN/dS (Human-Mouse Orthologs). dN/dS ratios of genes associated with model 2 random complexes are examined with respect to complex complexity and participation.

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Additional File 9:

Binned Plots for Figures 3D and 3F.3

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Additional File 10:

Protein complexes and dN/dS based on orthologs from a variety of species. dN/dS ratios of genes based on human-dog, human-chimp, human-rat, S. cerevisiae-S. mikatae and S. cerevisiae-S. paradoxus orthologs are examined with respect to complex complexity and participation.

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Additional File 11:

Complexes and gene conservation. The fraction of orthologs conserved in yeast and human complexes is examined against complex complexity.

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Additional File 12:

Extension and subsets of the protein complex data. Extended yeast complexes, complexes with subcomplexes removed, nuclear and non-nuclear complexes are examined with respect to complex complexity and participation.

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Additional File 13:

Analysis of protein complex data using the median. Analysis of protein complex data with respect to mean dN/dS ratios and sequence length is compared with analysis using the median.

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Additional File 14:

Homogeneity of Protein Properties in Yeast Complexes. Deviation in pI, secondary structure and evolutionary rate between proteins in annotated yeast complexes are compared to those in random complexes.

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Additional File 15:

Length difference of interacting proteins. Large proteins tend to interact with much smaller partners.

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