Back to Search
Start Over
Bioinformatical parsing of folding-on-binding proteins reveals their compositional and evolutionary sequence design.
- Source :
-
Scientific reports [Sci Rep] 2015 Dec 18; Vol. 5, pp. 18586. Date of Electronic Publication: 2015 Dec 18. - Publication Year :
- 2015
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Carrier Proteins chemistry
Databases, Factual
Humans
Hydrophobic and Hydrophilic Interactions
Molecular Sequence Data
Parathyroid Hormone-Related Protein chemistry
Parathyroid Hormone-Related Protein metabolism
Protein Folding
Protein Structure, Tertiary
Sequence Alignment
Carrier Proteins metabolism
Computational Biology
Evolution, Molecular
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 5
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 26678310
- Full Text :
- https://doi.org/10.1038/srep18586