Life Sciences Division

Movements within the nanosecond-to-millisecond window, which for proteins are considered slow, are a major research focus, as these movements are involved in biologically important processes, running from catalysis and signal transmission through to interactions between molecules and movements involving several domains of the same molecule. However, despite the importance of these movements, we still have only a rudimentary understanding of how they operate. Conventional methods based on computer simulations of molecular dynamics are unable to tackle these movements due to the sheer volume of calculations that would have to be performed in order to define, at atomic resolution, the different conformations (3D protein structures) adopted by a protein over a given timeframe.

An IBS (CEA, Grenoble) research team recently coupled new high-resolution NMR techniques with a novel simulation technique called molecular dynamics to determine the slow movements of a protein and map the conformations it naturally adopts. This protocol not only makes it possible to understand the role and distribution of protein domain movements over time-scales running from nanosecond up to millisecond, but also offers a breakthrough tool for tapping into the rich vein of data delivered by NMR.

Note: NMR is an equally powerful tool for determining the weaker interactions involved in the assembly and disassembly of protein complexes [find out more].

RMB spectra hold enormous potential for elucidating protein structure and dynamics. The IBS research team has developed new techniques for mapping the conformations a protein naturally adopts.