It is technically difficult to identify transport proteins, but here a method is presented that exploits the principle that they are stabilized in detergent solution when they bind their substrate.
Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.
A comprehensive approach to prediction of stabilizing mutations in G-protein coupled receptors yields high hit rate and crystal structures of 5HT2C in both active and inactive states.
A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.
Chemical perturbation-dependent deep mutational scanning data collected by a lab-based interdisciplinary graduate class resolves a paradox between the high evolution conservation and the high mutational tolerance of the protein ubiquitin.
Histone-lysine N-methyltransferase SETD3 (NP_115609.2) was identified as the actin-specific histidine N-methyltransferase, an enzyme catalyzing the extremely well-conserved methylation of H73 in β-actin.
By combining structure-based computational predictions and a thorough structural analysis, a highly thermostable enzyme, alcohol dehydrogenase, has been engineered.
Drug resistance in HIV is the result of mutations, which affect fitness depending on epistatic interactions with the entire sequence background that varies within and between patient populations.
T. gondii infection alters how peptide ligands are presented to the immune system by inducing a previously unreported structural change in Human Leukocyte Antigens (HLAs).
