Heme proteins--diversity in structural characteristics, function, and folding.

Journal article

The characteristics of heme prosthetic groups and their binding sites have been analyzed in detail in a data set of nonhomologous heme proteins. Variations in the shape, volume, and chemical composition of the binding site, in the mode of heme binding and in the number and nature of heme-protein interactions are found to result in significantly different heme environments in proteins with different functions in biology. Differences are also seen in the properties of the apo states of the prot...

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Authors: Smith, L; Kahraman, A; Thornton, J

• Publication status: Published
• Journal: Proteins
• Volume: 78
• Issue: 10
• Pages: 2349-2368
• Publication date: 2010-08-01
• DOI: 10.1002/prot.22747
• EISSN: 1097-0134
• ISSN: 0887-3585
• Language: English
• Keywords: Protein Binding; Humans; Heme; Models, Molecular; Hemeproteins; Bacterial Proteins; Protein Conformation; Computational Biology; Ligands; Animals; Apoenzymes; Binding Sites; Amino Acids; Protein Folding; Protein Stability; Holoenzymes; Databases, Protein