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A survey of the current drug screeni...

Dansereau, Stephen.

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A survey of the current drug screening techniques to obtain rational design and study drug -target interactions.

Record Type:	Electronic resources : Monograph/item
Title/Author:	A survey of the current drug screening techniques to obtain rational design and study drug -target interactions./
Author:	Dansereau, Stephen.
Description:	182 p.
Notes:	Source: Masters Abstracts International, Volume: 55-05.
Contained By:	Masters Abstracts International55-05(E).
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10131870
ISBN:	9781339896274

A survey of the current drug screening techniques to obtain rational design and study drug -target interactions.
Dansereau, Stephen.

A survey of the current drug screening techniques to obtain rational design and study drug -target interactions. - 182 p.

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

Thesis (M.S.)--State University of New York at Albany, 2016.

Different techniques have been developed over the years for the purpose of studying proteins and understanding their functions. Early techniques typically employed bioluminescence or fluorescence such such as the firefly protein luciferase and the jellyfish green fluorescent protein (GFP), respectively, to localize proteins within the cell. X-ray crystallography has also provided valuable structural details of many different proteins in vitro. Yet, nuclear magnetic resonance (NMR) spectroscopy offers the most realistic insight into proteins' physiologic structures and how proteins function in their native, cellular environments.

ISBN: 9781339896274Subjects--Topical Terms:

518028
Biochemistry.

A survey of the current drug screening techniques to obtain rational design and study drug -target interactions.
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020 $a 9781339896274
035 $a (MiAaPQ)AAI10131870
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100 1 $a Dansereau, Stephen. $3 3191445
245 1 2 $a A survey of the current drug screening techniques to obtain rational design and study drug -target interactions.
300 $a 182 p.
500 $a Source: Masters Abstracts International, Volume: 55-05.
500 $a Adviser: Alexander Shekhtman.
502 $a Thesis (M.S.)--State University of New York at Albany, 2016.
520 $a Different techniques have been developed over the years for the purpose of studying proteins and understanding their functions. Early techniques typically employed bioluminescence or fluorescence such such as the firefly protein luciferase and the jellyfish green fluorescent protein (GFP), respectively, to localize proteins within the cell. X-ray crystallography has also provided valuable structural details of many different proteins in vitro. Yet, nuclear magnetic resonance (NMR) spectroscopy offers the most realistic insight into proteins' physiologic structures and how proteins function in their native, cellular environments.
520 $a In-cell NMR spectroscopy is a technique that can exploit the nuclei of proteins in order to discern their structures and binding interactions in atomic resolution. This requires use of a chemical shift library or reference spectrum respectively, t o which the chemical shifts of the protein under study can be compared. The results offer real time analyses of proteins in their native, crowded cellular environments, making for more accurate data. The implications of unraveling a protein's structure are many, including understanding protein misfolding associated with pathologies, identifying a suitable therapeutic target, determining a biomolecules active site, studying protein-substrate interactions, all of which contribute to the rational design of drugs. These valuable insights are especially important in the treatment of both pathogenic and genetic diseases.
590 $a School code: 0668.
650 4 $a Biochemistry. $3 518028
650 4 $a Pharmacology. $3 634543
690 $a 0487
690 $a 0419
710 2 $a State University of New York at Albany. $b Chemistry. $3 1064619
773 0 $t Masters Abstracts International $g 55-05(E).
790 $a 0668
791 $a M.S.
792 $a 2016
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10131870