ArticleBiophysical journal2006
Structural diversity of protein segments follows a power-law distribution.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Complex evolutionary footprints revealed in an analysis of reused protein segments of diverse lengths.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Convergent evolution in structural elements of proteins investigated using cross profile analysis.BMC bioinformatics · 2012Article
- Word decoding of protein amino Acid sequences with availability analysis: a linguistic approach.PloS one · 2012Article
- Article
- Universal partitioning of the hierarchical fold network of 50-residue segments in proteins.BMC structural biology · 2009Article
- ProSeg: a database of local structures of protein segments.Journal of computer-aided molecular design · 2009Article
- Protein-segment universe exhibiting transitions at intermediate segment length in conformational subspaces.BMC structural biology · 2008Article
- Functionally important segments in proteins dissected using Gene Ontology and geometric clustering of peptide fragments.Genome biology · 2008Article
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2 authors.
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Abstract
The local structures of protein segments were classified and their distribution was analyzed to explore the structural diversity of proteins. Representative proteins were divided into short segments using a sliding L-residue window. Each set of local structures consisting of consecutive 1-31 amino acids was classified using a single-pass clustering method. The results demonstrate that the local structures of proteins are very unevenly distributed in the protein universe. The distribution of local structures of relatively long segments shows a power-law behavior that is formulated well by Zipf's law, implying that a protein structure possesses recursive and fractal characteristics. The degree of effective conformational freedom per residue as well as the structure entropy per residue decreases gradually with an increasing value of L and then converges to constant values. This suggests that the number of protein conformations resides within the range between 1.2L and 1.5L and that 10- to 20-residue segments are already proteinlike in terms of their structural diversity.
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