| Popis: |
Single-molecule fluorescence resonance energy transfer (smFRET) (reviewed in Munro et al., 2009) and cryo-electron microscopy (cryo-EM) investigations (Frank and Spahn, 2006; Spahn and Penczek, 2009; Fischer et al., 2010) of the translation apparatus reveal the ribosome’s propensity to undergo large-scale fluctuations in conformation during function. Progress in these areas, building upon achievements in high-resolution structure determination of ribosomal subunits and functional complexes of the ribosome (Yusupov et al., 2001; Wekselman et al., 2009: Zhang et al., 2009; Gao et al., 2009; Demeshkina et al., 2010; Stanley et al., 2010), combined with an ever increasing breadth of computational modeling, simulation (Sanbonmatsu and Tung, 2007; Whitford et al., 2010a), and bioinformatics approaches (Roberts et al., 2008; Alexander et al., 2010), offers the potential to further broaden our understanding of the dynamic nature of the ribosome and translation components during protein synthesis. The large fluctuations observed by single-molecule studies, and the multitude of conformations reported by cryo-EM, make it clear that each “state” of the ribosome is in fact an ensemble of structurally similar configurations that are localized to a particular minimum on the free-energy landscape. |
