The N-terminal receiver domain of NtrC is the molecular switch in the two-component signal
transduction. It is the first protein where structures of both the active (phosphyroylated) and …

The N-terminal receiver domain of protein NtrC (NtrCr) exhibits allosteric transitions between
the inactive (unphosphorylated) and active (phosphorylated) state on the microsecond time …

Receiver domains are key molecular switches in bacterial signaling. Structural studies have
shown that the receiver domain of the nitrogen regulatory protein C (NtrC) exists in a …

The dominant theory on the mechanism of response regulators activation in two-component
bacterial signaling systems is the “Y–T coupling” mechanism, wherein the χ 1 rotameric state …

The bacterial enhancer-binding protein NtrC activates transcription when phosphorylated on
aspartate 54 in its amino (N)-terminal regulatory domain or when altered by constitutively …

Multiple self‐guided Langevin dynamics (SGLD) simulations were performed to examine
structural and dynamical properties of the receiver domain of nitrogen regulatory protein C …

Protein actions are usually discussed in terms of static structures, but function requires
motion. We find a strong correlation between phosphorylation-driven activation of the …

Revised Manuscript Received November 15, 1994® abstract: NTRC is a transcriptional
enhancer binding protein whose N-terminal domain is a member of the family of receiver …

During Transitions Proteins Make Fleeting Bonds: Cell Skip to Main Content Advertisement
Cell This journal offers authors two options (open access or subscription) to publish research …

Recent successes in simulating protein structure and folding dynamics have demonstrated
the power of molecular dynamics to predict the long timescale behaviour of proteins. Here …