Anion Exchanger 1 (AE1) is the most abundant membrane protein in human red blood cells and the fastest known transporter. It plays a central role in facilitating carbon dioxide transport from tissues to the lungs by rapidly exchanging chloride and bicarbonate ions across the membrane. In collaboration with the Clarke Lab at Columbia University and using molecular dynamics simulations and advanced enhanced-sampling techniques with NAMD, the Resource researchers revealed the mechanism by which depletion of the anionic lipid PIP2 significantly lowers the rate of the transporter. Analysis of the simulations in VMD uncovered that the formation of a salt bridge between the lipid and AE1 residues modulates the transporter's structural dynamics and function. More details can be found in our publication in Nature Communications.
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- Drug-bound outward-facing conformation of a heterodimeric ABC exporter suggests a putative mechanism of drug translocation. Nat. Commun., 16:10403. 2025.
- Roles of the membrane-binding motif and the C-terminal domain of RNase E in localization and diffusion in E. coli. eLife, 14:RP105062. 2025.
- Ca2+ Stoichiometry Controls the Binding Mode of the PKCα C2 Domain to Anionic Membranes. J. Phys. Chem. B, 129(39):9893–9903. 2025.
- A to-do list for realizing the sequence-to-function paradigm of proteins. Curr. Opin. Struct. Biol., 93:103119. 2025.
- Voltage sensor conformations induced by LQTS-associated mutations in hERG potassium channels. Nat. Commun., 16:7126. 2025.
- Cryo-EM structure of the tissue factor/factor VIIa complex with a factor X mimetic reveals a novel allosteric mechanism. Blood, 2025.
- An Orchestrated Interaction Network at the Binding Site of Human SERT Enables the Serotonin Occlusion and Import. Biochemistry, 64(16):3652–3662. 2025.
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