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Open Access Highly Accessed Research article

Structural analysis of heme proteins: implications for design and prediction

Ting Li1, Herbert L Bonkovsky1234 and Jun-tao Guo5*

Author Affiliations

1 Cannon Research Center, Carolinas Medical Center, 1000 Blythe Boulevard, Charlotte, NC, 28203, USA

2 Department of Biology, University of North Carolina at Charlotte, Charlotte, NC, USA

3 Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA

4 Department of Medicine, University of Connecticut Health Center, Farmington, CT, USA

5 Department of Bioinformatics and Genomics, University of North Carolina at Charlotte, 9201 University City Boulevard, Charlotte, NC 28223, USA

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BMC Structural Biology 2011, 11:13  doi:10.1186/1472-6807-11-13

Published: 3 March 2011

Additional files

Additional file 1:

Datasets used in structural analysis of heme proteins. Table S1: a list of 125 non-redundant heme-binding protein chains; Table S2: heme and heme-like ligands in PDB; Table S3: heme proteins with multiple apo structures

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Additional file 2:

Comparative analysis of heme-binding proteins and non-heme proteins in terms of amino acid frequency, relative solvent accessibility, and Rvs (ratio between volume and area). Figure S1: relative frequencies of amino acids in non-redundant heme proteins; Figure S2: frequencies of relative solvent accessibility for heme interacting residues; Figure S3: heme binding pockets in EMMA (A) and 3CQVA (B); Figure S4: distribution of (A) Rvs (ratio between volume and area) and (B) nRvs (normalized Rvs) between heme binding pockets and non-heme binding pockets.

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