Abstract
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR-72701. Amid translation, newly synthesized polypeptides exiting ribosomes interact with chaperones and target factors that aid in polypeptide folding and transport. Ribosomal protein L23 sits upon the nascent polypeptide exit site of the 50S ribosomal subunit that structurally interacts with SRPs and TFs, among other surface proteins. L23 aids in the targeting and integration of light harvesting chloroplast particles, LHCPs, in the integration to Alb3 on the thylakoid membrane. This process of protein processing and targeting is not fully understood, nor how the protein reaches its final confirmation. As recombinant L23 has been found to aggregate and form inclusion bodies in E.coli. The present study is focused in developing a purification strategy for L23 to obtain a pure soluble refolded protein. The details of the purification and the characterization of the L23 will be presented.
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