During the second half of the 20th century, following structural biology hallmark works on
DNA and proteins, biochemists shifted their questions from “what does this molecule look …

The RAS-ERK pathway is a fundamental signaling cascade crucial for many biological
processes including proliferation, cell cycle control, growth, and survival; common across all …

Modification of the protein after synthesis (PTM) often affects protein function as supported
by numerous studies. However, there is no consensus about the degree of structural protein …

Phosphorylation carries chemical information in biological systems. In two-component
systems (TCSs), the sensor histidine kinase and the response regulator are connected …

Conformational changes are an essential feature for the function of some dynamic proteins.
Understanding the mechanism of such motions may allow us to identify important properties …

Previous studies of the protein kinase, ERK2, using NMR and hydrogen-exchange
measurements have shown changes in dynamics accompanying its activation by …

The activation loop segment in protein kinases is a common site for regulatory
phosphorylation. In extracellular signal-regulated kinase 2 (ERK2), dual phosphorylation …

Classical molecular dynamics (MD) simulations based on atomic models play an
increasingly important role in a wide range of applications in physics, biology, and …

The crucial role of TIR1‐receptor‐mediated gene transcription regulation in auxin signaling
has long been established. In recent years, the significant role of protein phosphorylation …

Structural changes involved in protein kinase activation and ligand binding have been
determined from a wealth of X-ray crystallographic evidence. Recent solution studies using …