Surface-enhanced Raman spectroscopy for drug discovery: peptide-RNA binding

Fundamental Determinants of the Accuracy of Equilibrium Constants for Affinity Complexes

“…The vast majority of equilibrium constants that are published in the scientific literature today are those of binding reactions involving large biological molecules and forming highly stable affinity complexes. − These equilibrium constants cannot be calculated because standard free energies of formation of typical interactants, such as proteins, DNA, drug leads, etc., are unknown. Therefore, equilibrium constants of affinity complexes are determined experimentally using a large scope of methods. − Most of these methods are supported by commercial instruments in which a researcher essentially loads the solutions into the instrument, pushes a button, and reads the resulting value with multiple significant figures and a small standard deviation.…”