Huajun Qin

TL;DR: The structure of the M2 conductance domain in a lipid bilayer is determined and it is proposed that the tetrameric His37-Trp41 cluster guides protons through the channel by forming and breaking hydrogen bonds between adjacent pairs of histidines and through specific interactions of the histidine with the tryptophan gate.

TL;DR: Seventy integral membrane proteins from the Mycobacterium tuberculosis genome have been cloned and expressed in Escherichia coli and expression levels were restricted to a narrow range of molecular weights and relatively few transmembrane helices.

TL;DR: Solid-state NMR data of the transmembrane domain of the M2 protein from influenza A virus are used to exemplify such conformational plasticity in a tetrameric helical bundle.

TL;DR: Exactly how well the native membrane needs to be modeled to achieve a native membrane protein structure is explored here, where the structure of the tetrameric M2 conductance domain (M2CD; residues 22–62; PDB #2L0J) that has been structurally characterized in synthetic lipid bilayers is validated.

TL;DR: This expression platform features high throughput cloning, high flexibility for different constructs, and high efficiency for membrane protein overexpression, and is expected to be useful in membrane protein structural and functional studies.