Kinetics articles from across Nature Portfolio

Here the authors perform modelling to reveal that the timescale of actin-VASP interactions plays a critical role in actin ring formation and filament length determines droplet deformation in VASP droplets: predictions from the model were tested against VASP GAB mutant.

Studying RNA decay remains a challenging task. Here, the authors present a technology that enables inducible rapid degradation of targeted mRNAs. Visualizing mRNA decay dynamics unveils insights into P-body function in RNA metabolism.

Understanding the molecular basis of voltage-sensing is of great importance in biology. Here, the authors use computational analysis and simulations to reveal atomic level insights into the mechanism of an isolated voltage-sensing domain.

The authors show G protein subtype selectivity at the β₁-adrenergic receptor is driven by the binding kinetics of ternary complex formation. Bound to G protein, the receptor adopts conformations that differ from its agonist-bound solution states.

Here the authors combine 19 F NMR and femtosecond transient absorption to characterise the structural origin of the multiphasic quenching dynamics in various species of BLUF domains, highlighting the importance of the heterogeneous active-site H-bond network.

How did the leopard get its spots? According to Rudyard Kipling’s 1902 children’s story, the leopard’s spots were created by fingerprints of an Ethiopian man. Fifty years later, Alan Turing laid the mathematical foundations of our understanding of leopard spots today.

In vitro Cas9-binding assays show the effects of mutations in the target sequence on binding kinetics.

Laurent Blanchoin reminds us of a seminal paper by Tom Pollard reporting the meticulous measurement of rate constants of actin assembly, and highlights its contribution to quantitative understanding of actin filament dynamics as well as its impact on his own research interests.

Contrary to conventional wisdom that molecular chaperones rely on hydrophobic interactions to bind a wide variety of client proteins in danger of misfolding, three recent studies reveal that the ATP-independent chaperone Spy exploits electrostatic interactions to bind its clients quickly, yet loosely enough to enable folding of the client while it is chaperone bound.

The fundamental mechanics of how EF-G catalyzes translocation of the mRNA and tRNA pairs on the ribosome has been intensely studied for over three decades. Two kinetic studies now reveal the sequence of events and the timing of key conformational changes in the ribosome during translocation and identify new intermediates in this complex process.