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ABC Transport Cycle Elucidated by Re...

Ramos, John E.

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ABC Transport Cycle Elucidated by Realtime Fluorescence Spectroscopy.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	ABC Transport Cycle Elucidated by Realtime Fluorescence Spectroscopy./
Author:	Ramos, John E.
Description:	63 p.
Notes:	Source: Dissertation Abstracts International, Volume: 72-05, Section: B, page: 2630.
Contained By:	Dissertation Abstracts International72-05B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3447953
ISBN:	9781124537269

ABC Transport Cycle Elucidated by Realtime Fluorescence Spectroscopy.
Ramos, John E.

ABC Transport Cycle Elucidated by Realtime Fluorescence Spectroscopy. - 63 p.

Source: Dissertation Abstracts International, Volume: 72-05, Section: B, page: 2630.

Thesis (Ph.D.)--Columbia University, 2010.

ABC Transporters are ubiquitous membrane spanning multi-domain proteins that are responsible for the trafficking of wide variety of small molecules including ions, amino acids, polysaccharides and lipids across the cellular membranes of virtually all organisms. A complete mechanistic model for the reaction cycle of ABC Transporters has remained elusive. While numerous biochemical and biophysical studies have provided insight into the manner in which ATP binding and hydrolysis control the conformation of their ATPase motor domains, there is little information available on how the motor domains drive unidirectional movement of transport substrates through their transmembrane domains. We have used fluorescence methods to monitor the kinetics of transport through a model ABC Transporter, including movement of the transport substrate relative to the protein complex. These studies were conducted on BtuCD-F, a vitamin B 12 transporter from E. coli, which is classified within the ABC superfamily as a type II importer. A visible fluorophore that is quenched by fluorescence resonance energy transfer (FRET) to vitamin B12 was attached to BtuF, the periplasmic binding protein domain of this transporter. The anisotropy of the fluorophore was used to monitor the association of BtuF with the transmembrane domains of BtuCD, while FRET to vitamin B12 was used to monitor movement of this substrate through wild-type and ATPase-deficient transporters incorporated into phospholipid bicelles. These studies provide a more detailed kinetic description of the transport cycle than previously available and demonstrate that the mechanochemical coupling between substrate translocation and the ATPase cycle differs substantially from models favored in the literature.

ISBN: 9781124537269Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

ABC Transport Cycle Elucidated by Realtime Fluorescence Spectroscopy.
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100 1 $a Ramos, John E. $3 1683778
245 1 0 $a ABC Transport Cycle Elucidated by Realtime Fluorescence Spectroscopy.
300 $a 63 p.
500 $a Source: Dissertation Abstracts International, Volume: 72-05, Section: B, page: 2630.
500 $a Adviser: John F. Hunt.
502 $a Thesis (Ph.D.)--Columbia University, 2010.
520 # $a ABC Transporters are ubiquitous membrane spanning multi-domain proteins that are responsible for the trafficking of wide variety of small molecules including ions, amino acids, polysaccharides and lipids across the cellular membranes of virtually all organisms. A complete mechanistic model for the reaction cycle of ABC Transporters has remained elusive. While numerous biochemical and biophysical studies have provided insight into the manner in which ATP binding and hydrolysis control the conformation of their ATPase motor domains, there is little information available on how the motor domains drive unidirectional movement of transport substrates through their transmembrane domains. We have used fluorescence methods to monitor the kinetics of transport through a model ABC Transporter, including movement of the transport substrate relative to the protein complex. These studies were conducted on BtuCD-F, a vitamin B 12 transporter from E. coli, which is classified within the ABC superfamily as a type II importer. A visible fluorophore that is quenched by fluorescence resonance energy transfer (FRET) to vitamin B12 was attached to BtuF, the periplasmic binding protein domain of this transporter. The anisotropy of the fluorophore was used to monitor the association of BtuF with the transmembrane domains of BtuCD, while FRET to vitamin B12 was used to monitor movement of this substrate through wild-type and ATPase-deficient transporters incorporated into phospholipid bicelles. These studies provide a more detailed kinetic description of the transport cycle than previously available and demonstrate that the mechanochemical coupling between substrate translocation and the ATPase cycle differs substantially from models favored in the literature.
590 $a School code: 0054.
650 # 4 $a Chemistry, Biochemistry. $3 1017722
650 # 4 $a Biophysics, General. $3 1019105
650 # 4 $a Operations Research. $3 626629
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690 $a 0786
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710 2 # $a Columbia University. $3 571054
773 0 # $t Dissertation Abstracts International $g 72-05B.
790 1 0 $a Hunt, John F., $e advisor
790 $a 0054
791 $a Ph.D.
792 $a 2010
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