id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-277318-cwuls6xs	Visscher, Koen	−1 Programmed Ribosomal Frameshifting as a Force-Dependent Process	2016-02-02		.txt	text/plain	8568	455	48	13 A recent single-molecule experiment indicates that ribosome helicase action during the translational elongation cycle may be twofold: it destabilizes the helical junction at the mRNA entry site favoring an open conformation, and it appears to pull mRNA strands apart during the translocation step when relatively large structural rearrangements occur on the ribosome. 26 We will review methods and experiments that apply force to the single molecules to determine the mechanical properties of codon-anticodon interaction at the slippery site, the stability of downstream mRNA structure motifs that give rise to −1 PRF, and elastic properties of the ssRNA elasticity bridging those elements. 104, 105 Single-molecule assays that probe the codon-anticodon dynamics at the slippery sequence and investigate the force dependence of the translation elongational cycle (discussed later in the chapter; see Fig. 8 ) should be fit to answer these questions and allow unfolding of −1 PRF mRNA structure motifs held at the ribosome's entry site.	./cache/cord-277318-cwuls6xs.txt	./txt/cord-277318-cwuls6xs.txt