The Statistical Conformation of a Highly Flexible Protein: Small-Angle X-Ray Scattering of S. aureus Protein A
Repository Usage Stats
Published Version (Please cite this version)10.1016/j.str.2014.06.011
Publication InfoCapp, JA; Hagarman, A; Oas, Terrence Gilbert; & Richardson, DC (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 http://hdl.handle.net/10161/11168.
This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
More InfoShow full item record
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