Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 46, Issue 2, Pages 87-91Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2009.10.003
Keywords
Cell-free protein synthesis; Elastin-like polypeptide (ELP); Protein expression profile; Recursive directional ligation (RDL) method; Repetitive polypeptides
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Funding
- Korea Government (MEST) [R01-2008-000-20516-0, KRF-2008-313-D00216, D00098]
- National Research Foundation of Korea [R01-2008-000-20516-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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An elastin-like polypeptide (ELP) fusion protein was expressed in a cell-free protein synthesis system, and the expression profile was analyzed quantitatively. By selective addition of specific amino acids constituting ELP molecules, the expression level of the ELP fusion protein was improved by 1.3-1.8 times as high as positive control. This result implies that the expression amount of long repetitive polypeptides, which was dramatically decreased in vivo system, can be compensated to a degree by adding repeatedly consumed amino acids in vitro system. Presented results demonstrate the potential of cell-free protein synthesis for high-throughput study of various repetitive polypeptides. (C) 2009 Elsevier Inc. All rights reserved.
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