Multiscale Conformational Heterogeneity in Staphylococcal Protein A: Possible Determinant of Functional Plasticity
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Published Version (Please cite this version)10.1016/j.str.2014.08.014
Publication InfoDeis, LN; Hagarman, A; Oas, Terrence Gilbert; Pemble IV, Charles W; Qi, Y; Richardson, DC; & Richardson, JS (2014). Multiscale Conformational Heterogeneity in Staphylococcal Protein A: Possible Determinant of Functional Plasticity. STRUCTURE, 22(10). pp. 1467-1477. 10.1016/j.str.2014.08.014. Retrieved from https://hdl.handle.net/10161/11166.
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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