Multi-step protein purification technique for crystallization
Pope, Albryona
2013
2010-2019
For years crystallization has been used to understand and identify the molecular structure of proteins. In order to obtain the best and most useful crystals from a particular protein and to properly identify its structure, it is necessary to purify the protein. The goal of this work is to develop a multistep purification technique for the purification of two specific proteins, mGO, modified glycolate oxidase, and SL06. This purification aims to isolate the protein from a complex mixture. Each protein is expressed in bacteria, His-Tagged, sonicated, and dialyzed in order to purify. SL06 is a dimeric receptor protein that is involved in the stress response of a tomato. When exposed to abscisic acid, a hormone known to induce plat stress, SL06 forms a complex and is known to exhibit differences in crystal structure. By identifying the crystal structure of SL06 and SL06-ABA complexes, the differences and similarities between the two structures can be examined.
text
application/pdf
conference proceedings
Enhancing Global Research and Education in STEM at Spelman College (G-STEM)
Spelman College
Georgia--Atlanta
http://hdl.handle.net/20.500.12322/sc.gstem:2013_pope_albryona
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