Long-Range Water Ordering between Intrinsically Disordered Proteins and Its Impact on Protein Diffusion.

Intrinsically disordered proteins (IDPs) play a critical role in the formation of membraneless organelles. The reduced diffusion of IDPs is associated with the stability of condensates and the related biological processes including phase separation and molecular recognition. Here we employ molecular dynamics simulations to investigate the diffusion dynamics of the LAF-1 RGG domains as well as their interplay with the solvent environment.

Salt-Tolerant Structure Features of Mussel Adhesive Proteins.

Mussel adhesive proteins have strong salt-tolerant adhesion ability and can assist marine mussels to firmly fix themselves on underwater structures. In our previous study, the adhesion ability of mussel adhesive proteins was largely attributed to the pair structure of Tyr/Dopa with basic residues (i.e.

Flexibility-Induced Collective Behavior Drives Symmetry Breaking in Discrimination of Undesired Ions.

Structure flexibility is essential for the biological function of proteins. At the same time, many proteins need to discriminate ligands with subtle differences, with one example being ion selectivity. Investigating the mechanisms by which flexible proteins achieve such precise discrimination is crucial for advancing our understanding of their functions.

Cryo-EM structures of the human cation-chloride cotransporter KCC1.

Cation-chloride cotransporters (CCCs) mediate the coupled, electroneutral symport of cations with chloride across the plasma membrane and are vital for cell volume regulation, salt reabsorption in the kidney, and γ-aminobutyric acid (GABA)-mediated modulation in neurons. Here we present cryo-electron microscopy (cryo-EM) structures of human potassium-chloride cotransporter KCC1 in potassium chloride or sodium chloride at 2.9- to 3.