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Use of Bionanotechnology to Decipher the Patterns of Assemblage and Interaction of Multi-Protein Complexes

Diaz, Manisha Regina
http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1250955267

Abstract Details

2009, Master of Science (MS), Bowling Green State University, Biological Sciences.
PAKs (p-21 activated kinases) are serine/threonine kinases that interact with the adaptor protein Nck-α through its Src homology3 (SH3) domains. Nck is an adaptor, i.e. its only function is to assemble two or more unlike proteins in a precise 3D orientation. Interaction of PAK and Nck-α has been reported to be mediated by the autophosphorylated state of the kinase. The amino-terminal portion of PAK has a sequence that binds Nck. An assay was designed using molecular genetics techniques to express Nck-α in Escherichia coli (E.coli) and capture Nck on PAK. Here, the bacterial lysate is used to place a gold-label on the Nck. Nck thus attached to 2 nm gold particles was retrieved by capturing it on PAK bound to 10 nm gold particles. Capture of gold-adsorbed Nck-α on gold-adsorbed PAK displayed patterns in the transmission electron microscope image indicating the interaction of PAK1 molecules with the Nck-α molecules. Several proteins from the bacterial lysate were captured along with Nck on PAK. Treatment of the bacterial lysate with anti-phosphotyrosine antibodies in order to block the interaction between the phosphotyrosine residues of the bacterial proteins and the Src homology (SH2) domain of Nck-α demonstrated that this type of interaction did not exist between these proteins. The results, however, suggested that Nck-α was captured on PAK-GST irrespective of the activity state of PAK. I conclude that it is possible to synthesize arrays consisting of one to many adsorbed gold particles around a single large particle, such as a quantum dot.
Carol Heckman, PhD (Advisor)
Donald Deters, PhD (Committee Member)
Roudabeh Jamasbi, PhD (Committee Member)
51 p.
Biology; Cellular Biology; Molecular Biology
Multi-Protein Complexes; Bionanotechnology; Patterns of Assemblage and Interaction of Multi-Protein Complexes

Recommended Citations

Citations

  • Diaz, M. R. (2009). Use of Bionanotechnology to Decipher the Patterns of Assemblage and Interaction of Multi-Protein Complexes [Master's thesis, Bowling Green State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1250955267

    APA Style (7th edition)

  • Diaz, Manisha. Use of Bionanotechnology to Decipher the Patterns of Assemblage and Interaction of Multi-Protein Complexes. 2009. Bowling Green State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1250955267.

    MLA Style (8th edition)

  • Diaz, Manisha. "Use of Bionanotechnology to Decipher the Patterns of Assemblage and Interaction of Multi-Protein Complexes." Master's thesis, Bowling Green State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1250955267

    Chicago Manual of Style (17th edition)

bgsu1250955267
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© 2009, all rights reserved.
This open access ETD is published by Bowling Green State University and OhioLINK.