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Protein interface classification by evolutionary analysis

Jose M Duarte1, Adam Srebniak2, Martin A Schärer13 and Guido Capitani1*

Author Affiliations

1 Paul Scherrer Institut, Villigen, CH-5232, Switzerland

2 SyBIT, ETH Zurich, Zurich, Switzerland

3 Present address: Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, CH-8093, Switzerland

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BMC Bioinformatics 2012, 13:334  doi:10.1186/1471-2105-13-334

Published: 22 December 2012

Additional files

Additional file 1:

Tables S1 and S2. Manually curated monomer and oligomer DC datasets, with experimental evidence from the literature. The "area" column refers to the largest interface in the protein crystal. References mostly given as PubMed id numbers linking to abstracts. Experimental evidence abbreviations used: SEC size exclusion chromatography; AUC analytical gel filtration; AUC (SV) analytical ultracentrifugation sedimentation velocity; SLS, DLS, LS (static/dynamic) light scattering; MALS multi-angle light scattering; MALLS multi-angle laser light scattering; CCL chemical cross-linking; FRET fluorescence resonance energy transfer; NMR nuclear magnetic resonance; SAXS small angle x-ray scattering; MS mass spectrometry; native-PAGE native polyacrylamide gel electrophoresis. (PDF 156 kb)

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