Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.

ABSTRACT: Proteins are highly variable biological systems, not only in their structures but also in their dynamics. The most extreme example of dynamics is encountered within the family of Intrinsically Disordered Proteins (IDPs), which are proteins lacking a well-defined 3D structure under physiological conditions. Among the biophysical techniques well-suited to study such highly flexible proteins, Site-Directed Spin Labeling combined with EPR spectroscopy (SDSL-EPR) is one of the most powerful, being able to reveal, at the residue level, structural transitions such as folding events. SDSL-EPR is based on selective grafting of a paramagnetic label on the protein under study and is limited neither by the size nor by the complexity of the system. The objective of this mini-review is to describe the b

SUBMITTER: Le Breton N 

PROVIDER: S-EPMC4436889 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature