A general property of disordered proteins is their structural expansion that results in a high macromolecular flexibility. Quasielastic incoherent neutron scattering (QENS) is a well-suited experimental method to study protein dynamics from the picosecond to several nanoseconds and in the Ångström length-scale. In QENS experiments of protein solutions hydrogens act as reporters for the motions...
Protein performs its biological functions by interacting with other proteins. Protein complexes, which are formed as a result of these interactions, consist of two or more components that associate along specific pathways - protein association pathways. The association pathway from monomer to oligomer is critical in a range of biological processes and thus it is of a vital importance to...
To obtain a molecular understanding of IDPs, a combined approach of experiments and simulations is useful. Recently we have shown that a coarse-grained model based on the primitive model, that has been used for modelling polyelectrolytes for over 30 years, works well for a range of IDPs where electrostatics governs the intra- and intermolecular interactions [1]. However, some IDPs have the...
Proteins are the most versatile constituents of the molecular machinery of life, and it is becoming increasingly clear that many of them perform essential functions even though they lack a well-defined folded structure. Single-molecule spectroscopy and fluorescence correlation spectroscopy provide an opportunity for investigating the molecular dynamics of these intrinsically disordered...
Over the last two decades, the classical structure-function paradigm has gradually been revisited with the discovery and the increasingly recognized importance of intrinsically disordered proteins (IDPs). IDPs do not rely on a well-defined three-dimensional structure to be functional, but rather exploit their intrinsic conformational dynamics for carrying out a wide range of biological...
The degree of compaction of the polypeptide chain is a property of key importance in intrinsically disordered proteins. Experimentally, compaction is often measured either by NMR (as the hydrodynamic radius) or SAXS (as the radius of gyration), and more detailed information may also be obtained by NMR paramagnetic relaxation enhancement measurements. A more detailed, atomic-level description...
A recent study by Subramani et al. (eLife, 2016) implied that the N-terminus of the magnesium transporter A (MgtA) protein (from hereon called Keif) is intrinsically disordered, but the advantage of this disordered feature to the function of the protein is still unknown. Thus, in this study, the structure of the Keif peptide part have been investigated by using both atomisic molecular...
