10.1371/journal.pcbi.1004578.g004 Silvia Lovera Silvia Lovera Maria Morando Maria Morando Encarna Pucheta-Martinez Encarna Pucheta-Martinez Jorge L. Martinez-Torrecuadrada Jorge L. Martinez-Torrecuadrada Giorgio Saladino Giorgio Saladino Francesco L. Gervasio Francesco L. Gervasio Free energy of the A-loop opening. Public Library of Science 2015 binding kinetics mutation imatinib resistance Kinase Conformational Dynamics T 315I gatekeeper Drug Resistance cancer patients tyrosine kinases ABL kinase domain dynamics simulations Myeloid leukemia microcalorimetry experiments DFG motif energy calculations binding mechanism energy landscape 2015-11-25 03:24:58 Figure https://plos.figshare.com/articles/figure/_Free_energy_of_the_A_loop_opening_/1612622 <p>Free energy surfaces of Abl, Src, and drug-resistant mutants projected on the optimal path describing the conformational change of the A-loop from open to closed in Src (CV1) and Abl (CV2). The free energy minima corresponding to an extended A-loop active-like conformation are labeled “A”, “B” is used for A-loop semi-closed (inactive) conformations and “C” for fully closed A-loop conformations. The contour lines are drawn every 1 kcal/mol.</p>