Ligand-protein Binding dynamics

III. Structure-based computational models of ligand-protein binding dynamics and molecular docking... 

In addition to being used for structural determinations of protein targets, NMR is increasingly being used to examine the dynamic interactions of ligand-receptor binding. Two NMR properties are particularly important chemical shift and nuclear spin relaxation. 

Serum albumin circulates in the blood stream transporting essential nutrients such as fatty acids to peripheral tissue. Transported molecules, called ligands, often have a special affinity for selected binding sites on proteins and nucleic acids. In this experiment, the dynamics of ligand-protein interactions will be explored with the binding of the dye phenol red to bovine serum albumin. The technique of gel filtration will be used to separate the dye-protein complex. Data will be analyzed in order to construct binding curves. 

Zhong, D., Douhal, A., and Zewail, A.H. (2000) Femtosecond studies of protein-ligand hydrophobic binding and dynamics human serum albumin Proc. Natl. Acad. Sci. 97, 14056-14061. 

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