ArticleTheoretical biology & medical modelling2007
Measuring the functional sequence complexity of proteins.
Article in Theoretical biology & medical modelling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Assessing, Testing and Estimating the Amount of Fine-Tuning by Means of Active Information.Entropy (Basel, Switzerland) · 2022Article
- Statistical discovery of site inter-dependencies in sub-molecular hierarchical protein structuring.EURASIP journal on bioinformatics & systems biology · 2012Article
- Dichotomy in the definition of prescriptive information suggests both prescribed data and prescribed algorithms: biosemiotics applications in genomic systems.Theoretical biology & medical modelling · 2012Review
- Is life unique?Life (Basel, Switzerland) · 2011Review
- Thermodynamic perspectives on genetic instructions, the laws of biology and diseased states.Comptes rendus biologies · 2011Article
- Biomolecular information gained through in vitro evolution.Biophysical reviews · 2010Review
- The capabilities of chaos and complexity.International journal of molecular sciences · 2009Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAbel and Trevors have delineated three aspects of sequence complexity, Random Sequence Complexity (RSC), Ordered Sequence Complexity (OSC) and Functional Sequence Complexity (FSC) observed in biosequences such as proteins. In this paper, we provide a method to measure functional sequence complexity. METHODS AND
resultsWe have extended Shannon uncertainty by incorporating the data variable with a functionality variable. The resulting measured unit, which we call Functional bit (Fit), is calculated from the sequence data jointly with the defined functionality variable. To demonstrate the relevance to functional bioinformatics, a method to measure functional sequence complexity was developed and applied to 35 protein families. Considerations were made in determining how the measure can be used to correlate functionality when relating to the whole molecule and sub-molecule. In the experiment, we show that when the proposed measure is applied to the aligned protein sequences of ubiquitin, 6 of the 7 highest value sites correlate with the binding domain.
conclusionFor future extensions, measures of functional bioinformatics may provide a means to evaluate potential evolving pathways from effects such as mutations, as well as analyzing the internal structural and functional relationships within the 3-D structure of proteins.
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