Shaw, Bryan Francis, 1976-Holden, Rebecca2015-05-282015-05-282015http://hdl.handle.net/2104/9365Charge regulation occurs when a protein modulates its net charge in a way that minimizes some perturbance, e.g. the binding of a metal cofactor. Net charge is a fundamental biophysical property that is nonetheless poorly characterized for many proteins. Although charge regulation has been observed in a handful of cases, the extent to which this phenomenon occurs, its mechanisms, and its function are not well understood (1,3). This study examined charge regulation in myoglobin in the transition between two redox states of the heme iron, oxy-Mb (Fe2+) and met-Mb (Fe3+). Protein charge ladders and capillary electrophoresis were used to measure the net charge of each myoglobin species (Zoxy-Mb and Zmet-Mb). It was determined that Zoxy-Mb = -1.67 ± 0.09, while Zmet-Mb = -1.02 ± 0.06. The difference between the net charge of these two states, 0.6 ± 0.1, was smaller than the expected 1.0 unit. The net charge of myoglobin was regulated by 0.4 ± 0.1 units in the transition between oxy-Mb and met-Mb. This study demonstrated the existence of charge regulation in myoglobin, suggesting that this phenomenon may be more widespread than previously considered.en-USBaylor University projects are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. Contact libraryquestions@baylor.edu for inquiries about permission.Net charge.Myoglobin.Protein charge ladders.Charge regulation.ThesisWorldwide access.Access changed 8/3/17.