Abstract
Editorial: Function and Flexibility: Friend or Foe?
Highlights
Specialty section: This article was submitted to Structural Biology, a section of the journal Frontiers in Molecular Biosciences
This research topic covers the impact of the study of protein flexibility on the structural biology field
Their work showcases how rigorous kinetic and structural analysis yields definitive conclusions that selectivity is a function of a conformational change after binding and the resulting slow dissociation rate of Gleevec from the Abl kinase, whereby the flexibility in the famous and highly conserved DFG-loop plays an important role (Agafonov et al, 2014; Wilson et al, 2015)
Summary
Specialty section: This article was submitted to Structural Biology, a section of the journal Frontiers in Molecular Biosciences. The high-resolution information that is obtained traditionally by x-ray crystallography or nuclear magnetic resonance (NMR) experiments is instrumental for understanding their functional properties, their biological roles, and their potential roles in diseases (“function follows form”). Many proteins even completely lack a well-defined 3D-structure under physiological conditions, the so-called intrinsically disordered proteins (IDPs).
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