Fig. 2
From: Exploring the potential role of GyrA inhibiting quinoline analog: an in silico study
Structural stability and flexibility analysis of gyrA wild (WT) and Mutants (MTs). (a) DCCM plot of gyrA WT. (b) Stabilizing and destabilizing mutations of all the mutants in the QRDR domain of gyrA protein. (c) Backbone flexibility in gyrA WT and all MTs, major focusing on QRDR domain (67–106). (d) The relative residue level fluctuation profile of gyrA WT and all MTs. Loss, and gain of intra-chain interactions due to mutations (e) gyrA WT and gyrA T83I MT (f) gyrA WT, gyrA D87G MT, gyrA D87N MT and gyrA D87Y MT (g) gyrA WT and gyrA T83I_D87N MT.
