Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 55, Issue 3, Pages 603-612Publisher
WILEY
DOI: 10.1002/prot.20043
Keywords
atom packing; crystal structure; electron transfer; protein interactions; recognition
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Interprotein electron transfer is characterized by protein interactions on the millisecond time scale. Such transient encounters are ensured by extremely high rates of complex dissociation. Computational analysis of the available crystal structures of redox protein complexes reveals features of the binding site that favor fast dissociation. In particular, the complex interface is shown to have low geometric complementarity and poor packing. These features are consistent with the necessity for fast dissociation since the absence of close packing facilitates solvation of the interface and disruption of the complex. (C) 2004 Wiley-Liss, Inc.
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