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Applications of Disulfide Tethering to Fragment Discovery and Protein Dynamics in Protein-Protein Interactions.

紀錄類型:	書目-語言資料,手稿 : Monograph/item
正題名/作者:	Applications of Disulfide Tethering to Fragment Discovery and Protein Dynamics in Protein-Protein Interactions./
作者:	Hallenbeck, Kenneth K.
面頁冊數:	1 online resource (156 pages)
附註:	Source: Dissertation Abstracts International, Volume: 79-09(E), Section: B.
Contained By:	Dissertation Abstracts International79-09B(E).
標題:	Biophysics. -
電子資源:	click for full text (PQDT)
ISBN:	9780355857825

Applications of Disulfide Tethering to Fragment Discovery and Protein Dynamics in Protein-Protein Interactions.
Hallenbeck, Kenneth K.

Applications of Disulfide Tethering to Fragment Discovery and Protein Dynamics in Protein-Protein Interactions. - 1 online resource (156 pages)

Source: Dissertation Abstracts International, Volume: 79-09(E), Section: B.

Thesis (Ph.D.)--University of California, San Francisco, 2018.

Includes bibliographical references

The study of protein protein-interactions (PPIs) can be approached with many lenses. Interaction networks can be mapped genetically or with proteomic methods. Biophysical characterization of specific partner interactions can clarify molecular mechanism of partner interaction. Screening methods can to identify novel interaction modulators, and site-directed chemical probes can used to demonstrate the importance of protein partner interaction in disease or biology. In this work I begin with an overview of the chemical biology toolbox for targeting non-catalytic cysteines residues. I apply one such tool, disulfide tethering, to two PPIs with the goal of broadening the PPIs which are targetable with covalent chemical probes. I then describe the use of cysteine-reactive molecules in understanding protein ligandability and its connection to protein dynamics. Finally, I study a promiscuous PPI receptor (Mac-1) to understand if inhibitors could be developed for specific ligands. Taken together, these data demonstrate the applicability of cysteine reactivity generally, and disulfide tethering specifically, to the study of PPIs.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2018

Mode of access: World Wide Web

ISBN: 9780355857825Subjects--Topical Terms:

581576
Biophysics.
Index Terms--Genre/Form:

554714
Electronic books.

Applications of Disulfide Tethering to Fragment Discovery and Protein Dynamics in Protein-Protein Interactions.
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502 $a Thesis (Ph.D.)--University of California, San Francisco, 2018.
504 $a Includes bibliographical references
520 $a The study of protein protein-interactions (PPIs) can be approached with many lenses. Interaction networks can be mapped genetically or with proteomic methods. Biophysical characterization of specific partner interactions can clarify molecular mechanism of partner interaction. Screening methods can to identify novel interaction modulators, and site-directed chemical probes can used to demonstrate the importance of protein partner interaction in disease or biology. In this work I begin with an overview of the chemical biology toolbox for targeting non-catalytic cysteines residues. I apply one such tool, disulfide tethering, to two PPIs with the goal of broadening the PPIs which are targetable with covalent chemical probes. I then describe the use of cysteine-reactive molecules in understanding protein ligandability and its connection to protein dynamics. Finally, I study a promiscuous PPI receptor (Mac-1) to understand if inhibitors could be developed for specific ligands. Taken together, these data demonstrate the applicability of cysteine reactivity generally, and disulfide tethering specifically, to the study of PPIs.
533 $a Electronic reproduction. $b Ann Arbor, Mich. : $c ProQuest, $d 2018
538 $a Mode of access: World Wide Web
650 4 $a Biophysics. $3 581576
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650 4 $a Pharmaceutical sciences. $3 1180569
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