id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-292985-w62xaa4f	Römer, Rudolf A.	Flexibility and mobility of SARS-CoV-2-related protein structures	2020-07-12		.txt	text/plain	5201	341	61	We are using a recent protein flexibility modelling approach, combining protein structural rigidity with possible motion consistent with chemical bonds and sterics. 34 We have performed our analysis through multiple conformational steps starting from the crystal structures of SARS-CoV-2-related proteins as currently deposited in the PDB. In Fig. 1 (a) we see that for the crystal structure of SARS-CoV-2 nucleocapsid protein N-terminal RNA binding domain (PDB:6m3m), the largest rigid cluster in the pristine structure, i.e. at E cut = 0, largely remains rigid through the dilution process of consecutively lowering E cut values. Last, a protein with 2nd-order rigidity should have the most complex behaviour in terms of flexibility since new possible mobility can be expected throughout the range of E cut values. Moving along directions proposed by an elastic normal model analysis of the crystal structure, we can therefore construct possible motion trajectories that are fully consistent with the bond network and steric constraints.	./cache/cord-292985-w62xaa4f.txt	./txt/cord-292985-w62xaa4f.txt