title: Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered proteins.
abstract: Intrinsically disordered proteins (IDPs) are predicted to represent a significant fraction of all functional proteins. Their inherent plasticity allows them to sample more efficiently their surroundings and thereby increase the probability of interaction with one or several different biological partners. Due to their high flexibility, IDPs cannot be represented by a single, three-dimensional structure; rather, an ensemble description can be invoked, where the protein is assumed to interconvert between different conformations. This chapter focuses on the use of NMR spectroscopy to characterize the dynamic behavior of IDPs, in particular residual dipolar couplings, that provide highly sensitive tools for the study of intrinsic structural propensity and conformational transitions accompanying protein function.
authors: Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, Grenoble, France.
authors: Loïc
authors: L
authors: Salmon
authors: Malene Ringkjøbing
authors: MR
authors: Jensen
authors: Pau
authors: P
authors: Bernadó
authors: Martin
authors: M
authors: Blackledge
mesh_terms: D000465:Algorithms; D000441:Hexanols / Q000737:chemistry; D050866:Liquid Crystals; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D010713:Phosphatidylcholines / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D000441:Hexanols; D008823:Micelles; D010713:Phosphatidylcholines; D011506:Proteins; D011092:Polyethylene Glycols