Wide-Line NMR Melting Diagrams, Their Thermodynamic Interpretation, and Secondary Structure Predictions for A30P and E46K α-Synuclein.

Parkinson's disease is thought to be caused by aggregation of the intrinsically disordered protein, α-synuclein. Two amyloidogenic variants, A30P, and E46K familial mutants were investigated by wide-line H NMR spectrometry as a completion of our earlier work on wild-type and A53T α-synuclein (Bokor M. et al.

Limitations of induced folding in molecular recognition by intrinsically disordered proteins.

Intrinsically disordered proteins (IDPs) exist and function without well-defined three-dimensional structures, thus they defy the classical structure-function paradigm. These proteins are common in proteomes, and they carry out essential functions often related to signalling and regulation of transcription. Herein, the experimental evidence for their lack of structure and the major functional benefits that structural disorder confers, are surveyed.