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.
Uversky, V., Santambrogio, C., Brocca, S., Grandori, R. (2012). Length-dependent compaction of intrinsically disordered proteins. FEBS LETTERS, 586(1), 70-73 [10.1016/j.febslet.2011.11.026].
Length-dependent compaction of intrinsically disordered proteins
SANTAMBROGIO, CARLO;BROCCA, STEFANIA;GRANDORI, RITA
2012
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.