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Glycan-Cyanovirin-N Interactions and Designed WW Domains: Combining Experimental and Computational Studies


Abstract Cyanovirin-N (CVN) is a cyanobacterial lectin with potent anti-HIV activity, mediated by binding to the N-linked oligosaccharide moiety of the envelope protein gp120. CVN offers a scaffold to develop multivalent carbohydrate-binding proteins with tunable specificities and affinities. I present here biophysical calculations completed on a monomeric-stabilized mutant of cyanovirin-N, P51G-m4-CVN, in which domain A binding activity is abolished by four mutations; with comparisons made to CVN<super>mutDB</super>, in which domain B binding activity is abolished. Using Monte Carlo calculations and docking simulations, mutations in CVN<super>mutDB</super> were considered singularly, and the mutations E41A/G and T57A were fo... (more)
Created Date 2014
Contributor Woodrum, Brian William (Author) / Ghirlanda, Giovanna (Advisor) / Redding, Kevin (Committee member) / Wang, Xu (Committee member) / Arizona State University (Publisher)
Subject Biochemistry / Biophysics / BP-Dock / cyanovirin-N / HIV / protein design / WW domain
Type Doctoral Dissertation
Extent 119 pages
Language English
Copyright
Reuse Permissions All Rights Reserved
Note Doctoral Dissertation Biochemistry 2014
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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Description Dissertation/Thesis