Intrinsically disordered proteins (IDPs) are macromolecules lacking unique 3D structures. In past two decades, it was revealed that a significant part of eukaryotic genome consists of IDPs. In spite of the absence of defined structures, IDPs are necessary for proper function of cells. (1.)
One of the largest IDPs studied with atomic reoslution is Microtubule Associated Protein 2c (MAP2c), that belongs to a MAP subfamily expressed in neurons during neuronal differentiation in the developing nervous system and can be found mainly in their dendrites (2.). MAP2c regulates dynamics and structure of microtubules in a phosphorylation-dependent manner, which is essential for the correct function of cytoskeleton of neural cells and its dysfunction may be one of the reasons of the development of neurodegenerative diseases (3.).
To understand the functions of MAP2c, knowledge of its conformational properties is required. NMR relaxation a powerful method well suited to provide information about dynamics of IDPs such as MAP2c. The relaxation study of MAP2c revealed presence of partially ordered regions that correlate well with known or proposed binding sites of the protein.