Protein side;chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein, protein-DNA, protein-RNA, and protein-cofactor interactions NMR spectroscopy has long been used to provide insights into the motions of side chain groups. Currently, the method of choice for studying side-chain dynamics by NMR is the measurement of methyl H-2 autorelaxation. Methyl H-2 autorelaxation exhibits simple relaxation mechanisms and can be straightforwardly converted to meaningful dynamic parameters. However, methyl groups can only be found in 6 of 19 side-chain bearing amino acids. Consequently, only a sparse assessment of protein side chain dynamics is possible. Therefore, there is a significant interest in developing novel methods of studying side chain motions that can be applied to all types of side-chains. Here, we show how side chain chemical shifts can be used to determine the magnitude of fast side chain motions in proteins. The chemical shift method is applicable to all side-chain bearing residues and does not require any additional measurements beyond standard NMR experiments for backbone and side-chain assignments.