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Proc Natl Acad Sci U S A. 2007 Jul 10;104(28):11627-32. Epub 2007 Jun 27.

The network of sequence flow between protein structures.

Author information

1
Department of Computer Science, Cornell University, Ithaca, NY 14853, USA.

Abstract

Sequence-structure relationships in proteins are highly asymmetric because many sequences fold into relatively few structures. What is the number of sequences that fold into a particular protein structure? Is it possible to switch between stable protein folds by point mutations? To address these questions, we compute a directed graph of sequences and structures of proteins, which is based on 2,060 experimentally determined protein shapes from the Protein Data Bank. The directed graph is highly connected at native energies with "sinks" that attract many sequences from other folds. The sinks are rich in beta-sheets. The number of sequences that transition between folds is significantly smaller than the number of sequences retained by their fold. The sequence flow into a particular protein shape from other proteins correlates with the number of sequences that matches this shape in empirically determined genomes. Properties of strongly connected components of the graph are correlated with protein length and secondary structure.

PMID:
17596339
PMCID:
PMC1913895
DOI:
10.1073/pnas.0701393104
[Indexed for MEDLINE]
Free PMC Article
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