Our research is focused on examining the structure and dynamics of proteins using NMR spectroscopy and developing methods to facilitate these studies. A particular emphasis is the investigation of proteins that undergo disorder-to-order transitions (Bracken, 2001). Insight into these structural changes is of central importance for understanding biological processes such as: determining how proteins adopt active structure; understanding how proteins interact with other molecules to transmit signals and/or effect chemical changes. Recent accomplishments include: methods for characterizing motional processes within proteins using NMR relaxation analysis (Kneller et.al. 2002); the development of improved protein production and isotopic labeling strategies (Marley et.al. 2001); the direct observation of protein folding and the unfolded state at atomic resolution (Cao et. al. 2004); and measurement of the energetic costs of restricting protein motions (Bracken et.al., 1999; Hill et.al, 2000). At present our lab is involved in several structural studies, aimed at determining the atomic structure and conformational changes necessary to confer biological activity.