Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The protonation state of Glu14 within the drug transporter EmrE is able to influence the conformational dynamics of the protein and thereby bias the inward-open conformation to facilitate substrate efflux.
Oscillations of actin, FBP17 and N-WASP are coupled to phase-shifted phosphoinositide (PI) turnover that is regulated by the lipid phosphatases SHIP1, synaptojanin 2 and PI 3-kinases. PI(4,5)P2 turnover regulates wave amplitude and PI(3,4)P2 acts as a pacemaker.
XSI analysis of two RNA kink-turn motifs, KtA and KtB, in a range of solution concentrations and in the presence of the kink-turn protein partner L7Ae reveals a restricted conformational ensemble that is regulated by ions and protein binding.
Point mutations in nascent peptides that regulate in the macrolide antibiotic resistance genes ermC and ermB can tune the recognition of the antibiotics erythromycin and telithromycin that control ribosome stalling and gene activation.