Bioinformatical parsing of folding-on-binding proteins reveals their compositional and evolutionary sequence design

Intrinsic disorder occurs when (part of) a protein remains unfolded during normal functioning. Intrinsically-disordered regions can contain segments that ‘fold on binding’ to another molecule. Here, we perform bioinformatical parsing of human ‘folding-on-binding’ (FB) proteins, into four subsets: Or...

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Bibliographic Details
Published in:Scientific reports 2015-12, Vol.5 (1), p.18586-18586, Article 18586
Main Authors: Narasumani, Mohanalakshmi, Harrison, Paul M
Format: Article
Language:English
Subjects:
631/114/470
631/114/663/2009
Amino Acid Sequence
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Computational Biology
Convergence
Databases, Factual
Discrimination
Evolution, Molecular
Humanities and Social Sciences
Humans
Hydrophobic and Hydrophilic Interactions
Hydrophobicity
Molecular Sequence Data
multidisciplinary
Parathyroid Hormone-Related Protein - chemistry
Parathyroid Hormone-Related Protein - metabolism
Protein Folding
Protein Structure, Tertiary
Proteins
Science
Sequence Alignment
Signal transduction
Trends
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Summary:Intrinsic disorder occurs when (part of) a protein remains unfolded during normal functioning. Intrinsically-disordered regions can contain segments that ‘fold on binding’ to another molecule. Here, we perform bioinformatical parsing of human ‘folding-on-binding’ (FB) proteins, into four subsets: Ordered regions, FB regions, Disordered regions that surround FB regions (‘Disordered-around-FB’) and Other-Disordered regions. We examined the composition and evolutionary behaviour (across vertebrate orthologs) of these subsets. From a convergence of three separate analyses, we find that for hydrophobicity, Ordered regions segregate from the other subsets, but the Ordered and FB regions group together as highly conserved and the Disordered-around-FB and Other-Disordered regions as less conserved (with a lesser significant difference between Ordered and FB regions). FB regions are highly-conserved with net positive charge, whereas Disordered-around-FB have net negative charge and are relatively less hydrophobic than FB regions. Indeed, these Disordered-around-FB regions are excessively hydrophilic compared to other disordered regions generally. We describe how our results point towards a possible compositionally-based steering mechanism of folding-on-binding.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep18586