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Hunting the Chameleon: Structural Conformations of the Intrinsically Disordered Protein Alpha‐Synuclein
Author(s) -
Drescher Malte,
Huber Martina,
Subramaniam Vinod
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200059
Subject(s) - intrinsically disordered proteins , context (archaeology) , alpha synuclein , chemistry , flexibility (engineering) , molecular dynamics , biophysics , conformational ensembles , protein structure , computational chemistry , biochemistry , biology , medicine , mathematics , disease , pathology , parkinson's disease , paleontology , statistics
To illustrate the potential of labeling approaches in the field of intrinsically disordered proteins (IDPs), studies on α‐synuclein (ASYN), one of the canonical model systems among the IDPs, are reviewed. ASYN displays a remarkable conformational flexibility, and depending on the molecular context, it adopts a variety of structurally distinct conformations resulting in the term “protein‐chameleon”.