The Statistical Conformation of a Highly Flexible Protein: Small-Angle X-Ray Scattering of S. aureus Protein A
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Published Version (Please cite this version)10.1016/j.str.2014.06.011
Publication InfoCapp, Jo A; Hagarman, Andrew; Richardson, David C; & Oas, Terrence G (2014). The Statistical Conformation of a Highly Flexible Protein: Small-Angle X-Ray Scattering of S. aureus Protein A. STRUCTURE, 22(8). pp. 1184-1195. 10.1016/j.str.2014.06.011. Retrieved from https://hdl.handle.net/10161/11168.
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Professor of Biochemistry
Our laboratory is primarily interested in the mechanisms of protein folding. We use nuclear magnetic resonance (NMR) and other types of spectroscopy to study the solution structure, stability and folding reactions of small protein models. These include monomeric λ repressor, the B domain of protein A (BdpA) and various regulator of G-protein signalling (RGS) domains. Our biophysical studies are used to inform our investigations of the role of folding mechanism in the function of pro