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Structural basis for ribosome recycling by RRF and tRNA
Zhou D, et al. Nat Struct Mol Biol 2020. Among authors: Gagnon MG. PMID 31873307
The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF). The molecular basis for ribosome recycling by RRF and EF-G remains unclear. Here, we report the crystal structure of a posttermination Thermus thermophilus 70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 Å. ...
The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycl …
Near-Atomic-Resolution Cryo-Electron Microscopy Structures of Cucumber Leaf Spot Virus and Red Clover Necrotic Mosaic Virus: Evolutionary Divergence at the Icosahedral Three-Fold Axes
Sherman MB, et al. J Virol 2020. Among authors: Smith TJ. PMID 31694952 Free PMC article.
Each capsid protein is comprised of three domains: R (RNA binding), S (shell), and P (protruding). Between the R domain and S domain is the "arm" region that studies have shown to play a critical role in assembly. ...
Each capsid protein is comprised of three domains: R (RNA binding), S (shell), and P (protruding). Between the R domain and S
The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly
Samuel PP, et al. Biophys J 2020. Among authors: White MA. PMID 32075750
Both unfolding experiments and independent small angle x-ray scattering measurements demonstrate that heme disassociation leads to the loss of tetrameric structural integrity. ...
Both unfolding experiments and independent small angle x-ray scattering measurements demonstrate that heme disassociation leads to th …
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