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FEBS Lett. 2012 Jan 2;586(1):70-3. doi: 10.1016/j.febslet.2011.11.026. Epub 2011 Nov 28.

Length-dependent compaction of intrinsically disordered proteins.

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Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, FL 33612, USA.


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.

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