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Single-Molecule Imaging of Conformat...

Kolster, Rachel Ann.

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Single-Molecule Imaging of Conformational Dynamics in a Neurotransmitter Transporter Homolog.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Single-Molecule Imaging of Conformational Dynamics in a Neurotransmitter Transporter Homolog./
Author:	Kolster, Rachel Ann.
Description:	95 p.
Notes:	Source: Dissertation Abstracts International, Volume: 77-08(E), Section: B.
Contained By:	Dissertation Abstracts International77-08B(E).
Subject:	Neurosciences. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10085659
ISBN:	9781339590844

Single-Molecule Imaging of Conformational Dynamics in a Neurotransmitter Transporter Homolog.
Kolster, Rachel Ann.

Single-Molecule Imaging of Conformational Dynamics in a Neurotransmitter Transporter Homolog. - 95 p.

Source: Dissertation Abstracts International, Volume: 77-08(E), Section: B.

Thesis (Ph.D.)--Columbia University, 2016.

Neurotransmitter:sodium symporter (NSS) proteins, the targets of antidepressants and psychostimulants, clear neurotransmitters from the synaptic cleft in a Na+-coupled transport mechanism. Transport is thought to occur via conformational rearrangements that alternately expose the substrate-binding site to each side of the membrane, but little is known about the mechanism by which ligand binding coordinates motions at the two faces. In this dissertation, single-molecule fluorescence resonance energy transfer (smFRET) techniques are used to image the dynamics of the prokaryotic NSS LeuT with sufficient resolution to describe the conformational states at both the intra- and extracellular faces for the first time. We found that the two sides do not move as a rigid body, contrary to popular models, and that previously undetected intermediate states are associated with transport activity. We also describe how ions and substrates influence conformational dynamics to create a productive transport cycle.

ISBN: 9781339590844Subjects--Topical Terms:

588700
Neurosciences.

Single-Molecule Imaging of Conformational Dynamics in a Neurotransmitter Transporter Homolog.
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245 1 0 $a Single-Molecule Imaging of Conformational Dynamics in a Neurotransmitter Transporter Homolog.
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500 $a Source: Dissertation Abstracts International, Volume: 77-08(E), Section: B.
500 $a Adviser: Jonathan Javitch.
502 $a Thesis (Ph.D.)--Columbia University, 2016.
520 $a Neurotransmitter:sodium symporter (NSS) proteins, the targets of antidepressants and psychostimulants, clear neurotransmitters from the synaptic cleft in a Na+-coupled transport mechanism. Transport is thought to occur via conformational rearrangements that alternately expose the substrate-binding site to each side of the membrane, but little is known about the mechanism by which ligand binding coordinates motions at the two faces. In this dissertation, single-molecule fluorescence resonance energy transfer (smFRET) techniques are used to image the dynamics of the prokaryotic NSS LeuT with sufficient resolution to describe the conformational states at both the intra- and extracellular faces for the first time. We found that the two sides do not move as a rigid body, contrary to popular models, and that previously undetected intermediate states are associated with transport activity. We also describe how ions and substrates influence conformational dynamics to create a productive transport cycle.
590 $a School code: 0054.
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650 4 $a Biophysics. $3 518360
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