Why are “natively unfolded” proteins unstructured under physiologic conditions?

By Vladimir N Uversky, J. R. Gillespie, A. Fink. Proteins: Structure, Function, and Bioinformatics, 2000

2,067 citations recorded by the source corpus.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c9bbebafd6a20d85eef9c94c4e6dec27719cab64

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Citations in the corpus

Natively Unstructured Loops Differ from Other Loops (2007, background): “net charge and low hydrophobicity [14,15], monitor the”
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. (2005, methodology): “This is in accordance with high net charge, and not simply the total charge, being one of the key determinants of disorder.(17) This interdependence of residues is manifest in the appearance of flavors of disorder.”
Natively unfolded proteins. (2005, background): “proteins that are completely disordered) are characterized by a unique combination of low overall hydrophobicity and high net charge [26].”
Intrinsic disorder in cell-signaling and cancer-associated proteins. (2002, positive): “The high ratio of charged to hydrophobic amino acid residues has been suggested as the likely cause of the observed disorder in these proteins.(32,33) Although the regulatory (851 proteins) and AfCS (2329 proteins) datasets differ quantitatively and qualitatively, we observed similar disorder predic”
LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana (2008, background): “The line marks the border between natively unstructured (left) and folded (right) proteins [91].”
Analysis of molecular recognition features (MoRFs). (2006, result): “This is similar to a previous description of intrinsically disordered proteins.(2) MoRFs also show lower proportions of aromatic amino acid residues in comparison with PDB_25 proteins, despite being enriched in phenylalanine.”