國立高雄大學圖資館 |

語系: 繁體中文

說明(常見問題)

圖資館首頁

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

A sequential expression system for i...

Stanford University.

A sequential expression system for identifying effectors of in vitro protein synthesis and folding.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	A sequential expression system for identifying effectors of in vitro protein synthesis and folding.
作者:	Woodrow, Kim Anh.
面頁冊數:	153 p.
附註:	Adviser: James R. Swartz.
附註:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5831.
Contained By:	Dissertation Abstracts International66-11B.
標題:	Biology, Molecular.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197528
ISBN:	9780542432262

A sequential expression system for identifying effectors of in vitro protein synthesis and folding.
Woodrow, Kim Anh.

A sequential expression system for identifying effectors of in vitro protein synthesis and folding. - 153 p.

Adviser: James R. Swartz.

Thesis (Ph.D.)--Stanford University, 2006.

Cell-free protein synthesis (CFPS) platforms based on cell extracts derived from Escherichia coli take advantage of the last 40 years of knowledge and experience in high-level recombinant protein expression in this model organism. They offer attractive alternatives to conventional fermentation methods for protein production. Identifying key reactions that enhance or inhibit in vitro protein synthesis and folding has led to improvements in CFPS energetics and reaction conditions. Continued development of CFPS as a platform for rapid and economical production of therapeutic proteins will benefit from our ability to identify factors that can improve in vitro expression and folding.

ISBN: 9780542432262Subjects--Topical Terms:

226919
Biology, Molecular.

A sequential expression system for identifying effectors of in vitro protein synthesis and folding.
LDR:03138nmm _2200289 _450 001 170972
005 20061228142335.5
008 090528s2006 eng d
020 $a 9780542432262
035 $a 00243002
040 $a UnM $c UnM
100 0 $a Woodrow, Kim Anh. $3 245003
245 1 2 $a A sequential expression system for identifying effectors of in vitro protein synthesis and folding.
300 $a 153 p.
500 $a Adviser: James R. Swartz.
500 $a Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5831.
502 $a Thesis (Ph.D.)--Stanford University, 2006.
520 # $a Cell-free protein synthesis (CFPS) platforms based on cell extracts derived from Escherichia coli take advantage of the last 40 years of knowledge and experience in high-level recombinant protein expression in this model organism. They offer attractive alternatives to conventional fermentation methods for protein production. Identifying key reactions that enhance or inhibit in vitro protein synthesis and folding has led to improvements in CFPS energetics and reaction conditions. Continued development of CFPS as a platform for rapid and economical production of therapeutic proteins will benefit from our ability to identify factors that can improve in vitro expression and folding.
520 # $a We have developed a method that uses sequential rounds of CFPS to identify proteins that influence in vitro transcription, translation, and protein folding. The first round of CFPS creates an array of cell extracts that are individually enriched with a single target protein. These proteins are expressed from linear DNA templates constructed in parallel using a PCR procedure wherein the overlap-extension reaction for the addition of transcription regulatory elements is separated from a GC-rich single-primer amplification of the full-length product. The expression templates are used to direct the first round of CFPS using a cell extract engineered to enhance linear DNA stability and using reaction conditions conducive for protein activation. After the first round of CFPS, the linear DNA templates are specifically targeted for degradation and a plasmid-based template for a reporter protein is added to initiate a subsequent round of protein expression. In this manner, the array is screened to identify targets that enhance or inhibit the expression and folding of the reporter protein. The culmination of this work has allowed us to identify proteins and biochemical activities that could improve the productivity of CFPS through rational metabolic engineering. This approach promises to broaden our understanding of cell-free biology and is also expected to provide a valuable platform technology for functional genomics.
590 $a School code: 0212.
650 # 0 $a Biology, Molecular. $3 226919
650 # 0 $a Biology, Microbiology. $3 226920
650 # 0 $a Engineering, Chemical. $3 226989
690 $a 0307
690 $a 0410
690 $a 0542
710 0 # $a Stanford University. $3 212607
773 0 # $g 66-11B. $t Dissertation Abstracts International
790 $a 0212
790 1 0 $a Swartz, James R., $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://libsw.nuk.edu.tw:81/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197528 $z http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3197528