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Studying the conformational landscap...

Rezaei Adariani, Soheila.

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Studying the conformational landscape of biomolecules using single molecule fluorescence spectroscopy.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Studying the conformational landscape of biomolecules using single molecule fluorescence spectroscopy./
Author:	Rezaei Adariani, Soheila.
Description:	81 p.
Notes:	Source: Masters Abstracts International, Volume: 55-05.
Contained By:	Masters Abstracts International55-05(E).
Subject:	Biophysics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10119397
ISBN:	9781339806310

Studying the conformational landscape of biomolecules using single molecule fluorescence spectroscopy.
Rezaei Adariani, Soheila.

Studying the conformational landscape of biomolecules using single molecule fluorescence spectroscopy. - 81 p.

Source: Masters Abstracts International, Volume: 55-05.

Thesis (M.S.)--Clemson University, 2016.

Proteins have many important functions in living system. They are produced from ribosomes as unstructured polypeptide chains of amino acids and then either fold by themselves or with the help of chaperones into their functional, three dimensional structures. However, the details for some proteins conformational changes and how it relates to their function, is still one of the unsolved questions in modern biophysics. Many techniques such as X-ray, NMR and single-molecule Forster Resonance Energy Transfer (smFRET) and multiparameter fluorescence detection techniques can get information about the protein conformational changes, structure, and also dynamic exchange and the equilibrium between different native protein states. Thus, providing insight into how those bio molecular machines really work. The focus of this thesis will therefore deal with: (1) protein structure and conformational changes (2) Fluorescence methods to study the protein conformational changes. (3) N-methyl-D-aspartate (NMDA) receptor that is, one member of the ionotropic glutamate receptor family, which requires a co-agonist such as glycine or D-serine for channel activation. Using fluorescence methods we studied the conformational changes of the ligand binding domain of this receptor in the presence of different co-agoinst to understand agonism.

ISBN: 9781339806310Subjects--Topical Terms:

518360
Biophysics.

Studying the conformational landscape of biomolecules using single molecule fluorescence spectroscopy.
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500 $a Source: Masters Abstracts International, Volume: 55-05.
500 $a Adviser: Hugo Sanabria.
502 $a Thesis (M.S.)--Clemson University, 2016.
520 $a Proteins have many important functions in living system. They are produced from ribosomes as unstructured polypeptide chains of amino acids and then either fold by themselves or with the help of chaperones into their functional, three dimensional structures. However, the details for some proteins conformational changes and how it relates to their function, is still one of the unsolved questions in modern biophysics. Many techniques such as X-ray, NMR and single-molecule Forster Resonance Energy Transfer (smFRET) and multiparameter fluorescence detection techniques can get information about the protein conformational changes, structure, and also dynamic exchange and the equilibrium between different native protein states. Thus, providing insight into how those bio molecular machines really work. The focus of this thesis will therefore deal with: (1) protein structure and conformational changes (2) Fluorescence methods to study the protein conformational changes. (3) N-methyl-D-aspartate (NMDA) receptor that is, one member of the ionotropic glutamate receptor family, which requires a co-agonist such as glycine or D-serine for channel activation. Using fluorescence methods we studied the conformational changes of the ligand binding domain of this receptor in the presence of different co-agoinst to understand agonism.
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