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[ subject:"Chemistry, Biochemistry." ]
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Mechanistic investigation of a CLC t...
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Brandeis University.
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Mechanistic investigation of a CLC transporter from Escherichia coli.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Mechanistic investigation of a CLC transporter from Escherichia coli./
作者:
Nguitragool, Wang.
面頁冊數:
97 p.
附註:
Adviser: Christopher Miller.
Contained By:
Dissertation Abstracts International69-01B.
標題:
Chemistry, Biochemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3295285
ISBN:
9780549399094
Mechanistic investigation of a CLC transporter from Escherichia coli.
Nguitragool, Wang.
Mechanistic investigation of a CLC transporter from Escherichia coli.
- 97 p.
Adviser: Christopher Miller.
Thesis (Ph.D.)--Brandeis University, 2008.
The mechanism of Cl- transport is a puzzle in membrane physiology that cannot be given undue attention. The single most common anion in living organisms, Cl- is not just a counter-ion of Na + and K+, but a physiologically essential chemical species whose membrane permeability controls the membrane potentials, regulates the cell volume, and modulates the pH of various intracellular vesicles. This dissertation concerns a single type of Cl- transport proteins called the CLC transporters. Unique among all known Cl- transporters, these proteins are exchangers that catalyze counter-transport of Cl - and H+. The article is focused on the mechanistic aspects of these proteins, utilizing as the model a CLC transporter of known structure from Escherichia coli, CLC-ec1. The goal is to establish the Cl-/H+ exchange stoichiometry and to examine the importance of the substrate-protein interaction as well as the cooperativity within the transporter's dimeric structure. The findings presented herein constitute an essential part of our understanding of CLC-ec1's transport mechanism, whose insight has taken us beyond the realm of bacterial physiology.
ISBN: 9780549399094Subjects--Topical Terms:
1017722
Chemistry, Biochemistry.
Mechanistic investigation of a CLC transporter from Escherichia coli.
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The mechanism of Cl- transport is a puzzle in membrane physiology that cannot be given undue attention. The single most common anion in living organisms, Cl- is not just a counter-ion of Na + and K+, but a physiologically essential chemical species whose membrane permeability controls the membrane potentials, regulates the cell volume, and modulates the pH of various intracellular vesicles. This dissertation concerns a single type of Cl- transport proteins called the CLC transporters. Unique among all known Cl- transporters, these proteins are exchangers that catalyze counter-transport of Cl - and H+. The article is focused on the mechanistic aspects of these proteins, utilizing as the model a CLC transporter of known structure from Escherichia coli, CLC-ec1. The goal is to establish the Cl-/H+ exchange stoichiometry and to examine the importance of the substrate-protein interaction as well as the cooperativity within the transporter's dimeric structure. The findings presented herein constitute an essential part of our understanding of CLC-ec1's transport mechanism, whose insight has taken us beyond the realm of bacterial physiology.
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http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3295285
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