Prediction of protein-protein interaction sites in intrinsically disordered proteins

HIGHLIGHTS

• who: September and collaborators from the University of Calcutta, India have published the research work: Prediction of protein-protein interaction sites in intrinsically disordered proteins, in the Journal: (JOURNAL)

SUMMARY

The commonly used experimental methods to pinpoint binding_sites in disordered proteins include nuclear magnetic_resonance spectroscopy (NMR) and nonequilibrium transient kinetic techniques (Mollica et_al, 2016). NMR identifies binding_sites through the changes in chemical shifts and residual dipole coupling (RDC) caused by changes in the magnetic environment during binding (Jensen et_al, 2011); non-equilibrium transient kinetic technique refers to identifying binding_sites by measuring the changes . . .

 



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