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Characterization of Small Metal-binding Protein (SmbP) From Nitrosomonas Europaea

Abstract A novel small metal-binding protein (SmbP), with only 93 residues and no similarity to other known proteins, has been isolated from the periplasm of Nitrosomonas europaea. It is characterized by its high percentage (17%) of histidines, a motif of ten repeats of seven residues, a four α-helix bundle structure, and a high binding affinity to about six equivalents of Cu2+. The goal of this study is to investigate the Cu2+ binding sites in SmbP and to understand how Cu2+ stabilizes the protein. Preliminary folding experiments indicated that Cu2+ greatly stabilizes SmbP. In this study, protein folding data from circular dichroism (CD) spectroscopy was used to elucidate the role of Cu2+ in stabilizing SmbP structure against unfolding in... (more)
Created Date 2010
Contributor Yan, Qin (Author) / Francisco, Wilson A (Advisor) / Allen, James (Committee member) / Ghirlanda, Giovanna (Committee member) / Arizona State University (Publisher)
Subject Chemistry / Biochemistry / Copper Binding / Nitrosomonas Europaea / Small Metal-binding Protein
Type Doctoral Dissertation
Extent 99 pages
Language English
Reuse Permissions All Rights Reserved
Note Ph.D. Chemistry 2010
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS

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Description Dissertation/Thesis