Whether a specific binding process can be studied by ITC is determined less by c (the product of binding constant K and titrand concentration [M]0) than by the total detectable heat qtot and the extent to which M can be converted to MX.
Two basic parameters of this binding site can be studied by kinetic and saturation analysis: the affinity of the ligand for its recognition site, the K d, and an estimate of the number of binding sites in a given tissue, the B max (Williams and Jacobson 1990).
For instance, by hybridizing with affinity-tagged oligodT, mRNA-binding proteome can be studied [37].
Since rigid body association occurs in a low dimensional space, the shape of the binding energy landscape can be studied in detail, in contrast to protein folding, which occurs in a very high dimensional space (Dill and Chan, 1997).
Effects of these predicted sequence changes on protein functions, including bindings with antiviral drugs and antibodies, can be studied in detail.
Experimentally determined protein-ligand structures can be studied to understand individual residue contributions towards ligand binding.
Ligand binding can be divided into specific and nonspecific binding.
Protein mutants with predicted high binding affinity or desired ligand specificity can then be studied experimentally.
SP and ME interactions and the corresponding binding interfaces can be directly studied by overlaying high-quality protein interaction data with known three-dimensional structures of protein complexes.
Drug binding mechanisms were studied.
