creator Wang, Yang advisor Zhang, Yu-Zhu In our study, the peanut allergen Ara h 5 was cloned from raw peanut mRNA. The cDNA of the gene was then introduced into different expression vectors for protein expression in different E.coli strains. Recombinant protein expression was very successful with useful amounts of soluble protein produced. Fast protein liquid chromatography was used to purify the recombinant Ara h 5. High purity protein was subjected to crystallization screen and good quality crystals were harvested. Several crystallographic data sets were collected at a synchrotron X-ray beam line. The three-dimensional structure of the peanut profilin Ara h 5 was determined to 1.10Å resolution. The purified protein and the purification methods can be used in future research on the protein’s allergenecity, cross-reactivity and allergy immunotherapies. The high resolution structure was compared with the structures of homologous allergens and the putative epitopes was displayed on the allergen structure to evaluate their possible legitimacies. In the future, the Ara h 5 structure could be very valuable in studies of allergenecity and in the design of future immunotherapies. Submitted by Liana Khananashvili (khananashvili@iit.edu) on 2013-05-22T16:45:58Z No. of bitstreams: 1 A20006026 Yang WANG PhD Thesis Signed Cover.pdf: 955940 bytes, checksum: ca5e90cf1ec0b2978e85868aea2bbd3c (MD5) Made available in DSpace on 2013-05-22T16:45:58Z (GMT). No. of bitstreams: 1 A20006026 Yang WANG PhD Thesis Signed Cover.pdf: 955940 bytes, checksum: ca5e90cf1ec0b2978e85868aea2bbd3c (MD5) Previous issue date: 2012-12 PH.D in Biology, December 2012 2012-11-21 2012-12 http://hdl.handle.net/10560/2987 en Dissertation born digital application/pdf In Copyright http://rightsstatements.org/page/InC/1.0/ Restricted Access ChBE / Chemical and Biological Engineering Illinois Institute of Technology Affiliated department