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Investigating the Specificity of Coiled-Coil Recognition.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Investigating the Specificity of Coiled-Coil Recognition./
作者:	Huey, Melina A.
面頁冊數:	1 online resource (168 pages)
附註:	Source: Masters Abstracts International, Volume: 82-11.
Contained By:	Masters Abstracts International82-11.
標題:	Molecular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28418537click for full text (PQDT)
ISBN:	9798728224877

Investigating the Specificity of Coiled-Coil Recognition.
Huey, Melina A.

Investigating the Specificity of Coiled-Coil Recognition. - 1 online resource (168 pages)

Source: Masters Abstracts International, Volume: 82-11.

Thesis (M.S.)--University of the Pacific, 2021.

Includes bibliographical references

The bZIP transcription factors make up a family of long α-helical proteins that dimerize based on a pattern of hydrophobic residues and bind to DNA through a region of basic residues. Because binding specificity is a particular topic of interest, the dimerization interaction is attractive as a possible candidate to better understand protein quaternary structure. Use of the Knob-Socket (KS) model for determination of packing structure provides a novel approach to analyze protein-protein interactions. A KS analysis of the protein-protein interface provides unique insight into the specificity of the classical leucine zipper pseudo-7mer repeat. From an analysis of the KS packing maps, this research provides evidence of a general framework for defining the specificity between coiled-coils. The KS maps show how hydrophobic specificity is defined in the coiled-coil interface, where knobs are centralized in the middle of the socket packing, while the peripheral socket residues are hydrophilic. Based on this KS analysis, the KS model will be used to design proteins that mimic the leucine zipper region of bZIP proteins. The proteins will be purified into E. coli and its 2° structure will be confirmed through circular dichroism. Binding specificity will be studied through mutations of the designed proteins and compared using the BACTH (bacterial adenylate cyclase two-hybrid) system.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9798728224877Subjects--Topical Terms:

517296
Molecular biology.
Subjects--Index Terms:

Coiled-Coil recognitionIndex Terms--Genre/Form:

542853
Electronic books.

Investigating the Specificity of Coiled-Coil Recognition.
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245 1 0 $a Investigating the Specificity of Coiled-Coil Recognition.
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500 $a Source: Masters Abstracts International, Volume: 82-11.
500 $a Advisor: Tsai, Jerry.
502 $a Thesis (M.S.)--University of the Pacific, 2021.
504 $a Includes bibliographical references
520 $a The bZIP transcription factors make up a family of long α-helical proteins that dimerize based on a pattern of hydrophobic residues and bind to DNA through a region of basic residues. Because binding specificity is a particular topic of interest, the dimerization interaction is attractive as a possible candidate to better understand protein quaternary structure. Use of the Knob-Socket (KS) model for determination of packing structure provides a novel approach to analyze protein-protein interactions. A KS analysis of the protein-protein interface provides unique insight into the specificity of the classical leucine zipper pseudo-7mer repeat. From an analysis of the KS packing maps, this research provides evidence of a general framework for defining the specificity between coiled-coils. The KS maps show how hydrophobic specificity is defined in the coiled-coil interface, where knobs are centralized in the middle of the socket packing, while the peripheral socket residues are hydrophilic. Based on this KS analysis, the KS model will be used to design proteins that mimic the leucine zipper region of bZIP proteins. The proteins will be purified into E. coli and its 2° structure will be confirmed through circular dichroism. Binding specificity will be studied through mutations of the designed proteins and compared using the BACTH (bacterial adenylate cyclase two-hybrid) system.
533 $a Electronic reproduction. $b Ann Arbor, Mich. : $c ProQuest, $d 2023
538 $a Mode of access: World Wide Web
650 4 $a Molecular biology. $3 517296
650 4 $a Biochemistry. $3 518028
650 4 $a Biophysics. $3 518360
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653 $a Leucine zipper pseudo-7mer repeat
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