| Summary: | Here we hypothesize that some proteins use their structured N-terminal domains (SNTDs) to organize the remaining protein chain by means of intramolecular interactions, so generating partially condensed proteins. This model has several attractive features: as the nascent protein chain emerges from the ribosome, the SNTD folds spontaneously and then serves as a nucleation point for the yet unstructured amino acid chain, creating more compact shapes. This reduces the risk of protein degradation or aggregation. Moreover, an interspersed pattern of SNTD-docked regions and free loops can coordinate assembly of sub-complexes in defined loop-sections and enables novel regulatory mechanisms, for example through posttranslational modifications of docked regions.
|
|---|