Robbins Puthenveetil

TL;DR: Current approaches and technological developments in the determination of membrane protein structures by solution NMR are discussed and recent structural and mechanistic insights gained with this technique are highlighted.

TL;DR: This paper presents an on-column method for nanodisc preparation with multiple strategies and discusses the potential use of alternative nanoscale phospholipid bilayer systems like styrene maleic acid lipid disc and saposin-A lipoprotein disc.

TL;DR: Results show that ligand binding to BTN3A1 induces a conformational change within the intracellular domain that involves the JM region and is required for full activation of Vγ9Vδ2 T cells.

TL;DR: This work has made nanodiscs more suitable for solution NMR applications by reducing the diameter of the self‐assembly complex to its potential limit and presents an on‐column method for a rapid, efficient, single‐step preparation of protein incorporated nanodISCs at high concentrations.

TL;DR: It is shown that TprI also possesses bipartite architecture, trimeric structure, and porin function and that the MOSPC-like domains of native TprC and TPRI are surface-exposed in T. pallidum, whereas their MOSPN- like domains are tethered within the periplasm.