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Dynamics of G protein conformational changes and subunit interactions.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Dynamics of G protein conformational changes and subunit interactions./
作者:	Yang, Chii-Shen.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 1998,
面頁冊數:	155 p.
附註:	Source: Dissertations Abstracts International, Volume: 60-09, Section: B.
Contained By:	Dissertations Abstracts International60-09B.
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9915040
ISBN:	9780599137486

Dynamics of G protein conformational changes and subunit interactions.
Yang, Chii-Shen.

Dynamics of G protein conformational changes and subunit interactions. - Ann Arbor : ProQuest Dissertations & Theses, 1998 - 155 p.

Source: Dissertations Abstracts International, Volume: 60-09, Section: B.

Thesis (Ph.D.)--University of Illinois at Chicago, Health Sciences Center, 1998.

This item must not be sold to any third party vendors.

This thesis was focused on the study of intra-molecular conformational changes in the α subunit of heterotrimeric G protein as well as inter-molecular interactions with other proteins. We first developed a fluorescently tagged Gα subunit. The labeling sites for fluorescent probes on Gα were identified to be Cys210 and Cys347. Furthermore, the labeled Gα proteins were shown to have no important loss of function except receptor-catalyzed guanine nucleotide exchange in certain mutants. In the intra-molecular conformational change studies, both amino- and carboxyl-terminus of Gα were found to undergo conformational changes during Gα activation. These observations suggest conformational changes upon GTP binding to Gα are at least partially responsible for the decreased affinity of Gα-GTP to both receptor and Gβγ. Based on those findings, we propose a more detailed model for G protein activation and deactivation cycle, which suggests that Gα exists in at least three conformational states during the course of the entire G protein cycle. It is also shown that the fluorescence Gα is sensitive to Gβγ, RGS and PDEγ interactions. Thus these fluorescent studies have provided us with new insights into the dynamics of G protein conformational changes during its activation/inactivation cycle in signal transduction.

ISBN: 9780599137486Subjects--Topical Terms:

518360
Biophysics.
Subjects--Index Terms:

Conformational changes

Dynamics of G protein conformational changes and subunit interactions.
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500 $a Source: Dissertations Abstracts International, Volume: 60-09, Section: B.
500 $a Publisher info.: Dissertation/Thesis.
500 $a Advisor: Hamm, Heidi E.
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506 $a This item must not be sold to any third party vendors.
506 $a This item must not be added to any third party search indexes.
520 $a This thesis was focused on the study of intra-molecular conformational changes in the α subunit of heterotrimeric G protein as well as inter-molecular interactions with other proteins. We first developed a fluorescently tagged Gα subunit. The labeling sites for fluorescent probes on Gα were identified to be Cys210 and Cys347. Furthermore, the labeled Gα proteins were shown to have no important loss of function except receptor-catalyzed guanine nucleotide exchange in certain mutants. In the intra-molecular conformational change studies, both amino- and carboxyl-terminus of Gα were found to undergo conformational changes during Gα activation. These observations suggest conformational changes upon GTP binding to Gα are at least partially responsible for the decreased affinity of Gα-GTP to both receptor and Gβγ. Based on those findings, we propose a more detailed model for G protein activation and deactivation cycle, which suggests that Gα exists in at least three conformational states during the course of the entire G protein cycle. It is also shown that the fluorescence Gα is sensitive to Gβγ, RGS and PDEγ interactions. Thus these fluorescent studies have provided us with new insights into the dynamics of G protein conformational changes during its activation/inactivation cycle in signal transduction.
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