자료유형  

 학위논문

Control Number  

0014996731

International Standard Book Number  

9780438206229

Dewey Decimal Classification Number  

660

Main Entry-Personal Name  

Pearson, C. Seth.

Publication, Distribution, etc. (Imprint  

[Sl] : Rensselaer Polytechnic Institute, 2018

Publication, Distribution, etc. (Imprint  

Ann Arbor : ProQuest Dissertations & Theses, 2018

Physical Description  

102 p

General Note  

Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.

General Note  

Advisers: Georges Belfort

Dissertation Note  

Thesis (Ph.D.)--Rensselaer Polytechnic Institute, 2018.

Summary, Etc.  

요약Inteins are protein elements that autocatalytically excise themselves from a host protein in a process called protein splicing. The two flanking sequences of the host protein, called the N- and C-exteins, are subsequently ligated with a native p

Summary, Etc.  

요약During this process, the intein breaks two peptide bonds and forms a third. Taking advantage of the intein's ability to catalyze these reactions, both within the natural host as well as in vitro for biotechnological applications, provides an att

Summary, Etc.  

요약Our work focuses on two of the three inteins found in the human pathogen Mycobacterium tuberculosis (Mtu), RecA and SufB. The intein-interrupted proteins are important for the viability of Mtu. Preventing intein excision, and thus the formation

Summary, Etc.  

요약Turning to methods of control for in vitro applications, we introduced a mutation in Mtu RecA that causes the intein to spontaneously form a thiazoline ring at the N-terminal splicing junction. While present, the thiazoline ring prevents any fur

Summary, Etc.  

요약The final aspect of our work is based on the intriguing hypothesis that inteins are not simply parasitic elements, but offer a beneficial protein-level control of host protein function. We demonstrated that Mtu SufB activity is inhibited in vivo

Summary, Etc.  

요약Overall, this work investigates strategies for controlling inteins in the realms of drug development, protein purification, and host regulation and stress response.

Subject Added Entry-Topical Term  

Chemical engineering

Subject Added Entry-Topical Term  

Biochemistry

Added Entry-Corporate Name  

Rensselaer Polytechnic Institute Chemical Engineering

Host Item Entry  

Dissertation Abstracts International. 79-12B(E).

Host Item Entry  

Dissertation Abstract International

Electronic Location and Access  

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Control Number  

joongbu:553206