How does one protein recognize and bind with its partner? It is the physical attraction and the right amount of luck that two proteins come together to function in unison. My research focuses on understanding how a protein’s unique 3D fold helps its to function. A class of proteins that I am most interested in are chemokines. These highly conserved, solubly expressed proteins function to direct cell migration in vivo and regulate a variety of different cellular processes. Two chemokine networks that I study are CXCL12/CXCR4 and CCCL20/CCR6. The unique biology of having two distinct functions for either the monomeric or dimeric forms of CXCL12, make this chemokine one of the most studied and interesting proteins in the field. The chemokine, CCL20, shares a similar dimeric conformation and other physical characteristics with CXCL12. The availability of two distinct biological functions for dimer and monomer has yet to be found but represent a new, exciting signaling pathway in the progression of psoriasis. I use NMR spectroscopy to deconvolute the complex interactions between chemokines and their receptors. Solving 3D NMR structures, analyzing protein-protein interactions and medium-throughput drug screening are some ways that I use NMR in the search of chemokine small molecule ligands. Understanding the way a chemokine binds to its receptor, helps guide our in silico docking and virtual screening to eventually analyze by NMR. In addition to NMR, I use cell-based assays and animal models to evaluate and validate molecules that are promising for future development. In our lab, we use a variety of physical chemistry, cell biology and in silico docking techniques to understand and manipulate chemokine function with small molecule ligands.