β Scribed by Hang Yin
No coin nor oath required. For personal study only.
Although membrane proteins account for approximately one third of all proteins encoded in the human genome, the functions and structures of their transmembrane domains are much less understood than the waterβsoluble regions. A major hurdle in studying these transmembrane domains is the lack of appropriate exogenous agents that can be used as specific probes. Despite the daunting challenges, major strides have recently been made in targeting the transmembrane domains of a variety of membrane proteins. High affinity and selectivity have been achieved in model biophysical systems, membranes of bacteria, and mammalian cells.
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Nanosecond molecular dynamics simulations in a fully solvated phospholipid bilayer have been performed on single transmembrane β£-helices from three putative ion channel proteins encoded by viruses: NB (from influenza B), CM2 (from influenza C), and Vpu (from HIV-1). β£-Helix stability is maintained w
Nef is a multifunctional gene of HIV which can increase virus replication either directly or by modulating the target cell's metabolism. Nevertheless the role of the exogenous Nef protein is not yet well understood. To investigate it, we studied the eects of the recombinant Nef protein on the expres
Aminoglycosides are a structurally diverse family of aminosugar and aminocyclitol derivatives that are currently the only well-characterized class of small molecules that selectively bind RNA, [1] including sites on prokaryotic 16S rRNA which is believed to be the locus of aminogylcoside antibiotic