conformational isomerism

Advertising and content can be personalised based on your profile. Your activity on this service can be used to build or improve a profile about you for personalised advertising and content. Advertising and content performance can be measured. Reports can be generated based on your activity and those of others. Your activity on this service can help develop and improve products and services. 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. DNA’s physical properties are key to gene regulation and protein binding. Here, authors use massive simulations to map all 2,080 unique DNA hexamers, revealing a “physical code” that explains how sequence mechanics shape genome evolution. Drebrin regulates crucial cellular processes through its F-actin binding and regulating functions. Here, the authors report cryo-EM structures of drebrin’s actin-binding domains complexed with F-actin, giving mechanistic insight into its F-actin regulatory activities. Henipaviruses are a group of emerging human pathogens including the deadly Nipah virus. Here, the authors biochemically, biophysically, and structurally investigate the antigenicity and functionality of their surface glycoproteins. Wnt morphogens are released from signaling cells in complex with carrier proteins, to offset insolubility due to lipidation. Here, the authors dissect the mechanism of Wnt release and show it is governed by conformational cycling of the G-protein-coupled receptor-like transporter Wntless. Ribosomes are crucial for protein synthesis and managing cellular stress. Here, authors show that ribosomal protein L11 acts as a global regulator, coordinating complex internal signaling to ensure proper bacterial survival during environmental stress. Yasuhisa Mizutani marvels at how effectively nature utilizes the π -conjugated system of retinal in proteins. NMR spectroscopy is a critical tool for linking protein structure, dynamics and interactions to protein function, but is challenging to apply to high-molecular-weight proteins. The chemical synthesis of an NMR probe combines the advantages of four different nuclei, 1H, 2H, 13C and 19F, to achieve optimal resolution for these larger systems. An infrared laser-induced temperature jump provides a rapid and broadly applicable perturbation to protein dynamics. Temperature-jump crystallography was paired with time-resolved X-ray crystallography to study the dynamic enzyme lysozyme. Measurements with and without a functional inhibitor revealed different patterns in the propagation of motion throughout the enzyme. Complexity is a hallmark of biological systems, but scientific experiments are typically conducted in simplified conditions. Now, diverse polymers that mimic the local environments of complex biological mixtures have been shown to improve protein folding, stability and function. Although critically important for protein function, post-translational modifications are complex and notoriously difficult to study. Now, the effects of O-GlcNAcylation on chaperone activity and the accompanying inhibition of amyloid fibril formation have been revealed, potentially yielding new routes to combat neurodegeneration.