id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-002439-wesyiymn	Le, My-Tra	Folding behavior of a T-shaped, ribosome-binding translation enhancer implicated in a wide-spread conformational switch	2017-02-13		.txt	text/plain	12389	589	60	For this current report, optical tweezers (OT), a type of single molecule force spectroscopy, and steered molecular dynamic simulations (SMD) were used to examine the folding/unfolding pathways of the TSS. One possibility for why the TSS-only fragment was not stable was the omission of the upstream 5A, as it was subsequently shown that adjacent doublet mutations in 5A (positions 8 and 9 in Figure 1A ) or single mutations disrupting É 3 caused identical enhancements in flexibility of residues throughout the 5A/H4a/É 3 region as assayed Hairpins H4a, H4b and H5 and tertiary interactions É 2 and É 3 comprise the TSS. Initial explicit solvent SMD simulations performed on fragment TSS108 (C 5 through A 112 ) at pulling speeds of 1.0 Å /ps and 0.5 Å /ps terminated with H5 and H4b helices remaining partly basepaired, indicating that the RNA chain was ahead of its approximate equilibrium state.	./cache/cord-002439-wesyiymn.txt	./txt/cord-002439-wesyiymn.txt