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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1002/prot.22747

Authors


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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Kahraman, A More by this author
Thornton, JM More by this author
Journal:
Proteins
Volume:
78
Issue:
10
Pages:
2349-2368
Publication date:
2010-08-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:8799e188-48ae-4e15-a8d8-1eb5e0fc9be4
Source identifiers:
60472
Local pid:
pubs:60472

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