Length-dependent Compaction of Intrinsically Disordered Proteins
Document Type
Article
Publication Date
2012
Keywords
Compaction Index, Hydrodynamic Radius, Induced Folding, Functional Misfolding, Structural Disorder, Sic1
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.febslet.2011.11.026
Abstract
This work investigates the effect of chain length on the degree of compaction of intrinsically disordered proteins (IDPs). The three main IDP types, native coil (NC), pre-molten globule (PMG) and molten globule (MG), are compared by means of a compaction index (CI) normalized for chain length. The results point out a strong variability of compactness as a function of chain length within each group, with larger proteins populating more compact states. While qualitative sequence features are responsible for the main differences among groups, chain length seems to have an unspecific effect modulating the extent of compaction within each group. The results are consistent with a cooperative character of the weak interactions responsible for chain collapse.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 586, issue 1, p. 70-73
Scholar Commons Citation
Uversky, Vladimir N.; Santambrogio, Carlo; Brocca, Stefania; and Grandori, Rita, "Length-dependent Compaction of Intrinsically Disordered Proteins" (2012). Molecular Medicine Faculty Publications. 496.
https://digitalcommons.usf.edu/mme_facpub/496
