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Investigation of factors contributin...

Robic, Srebrenka.

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Investigation of factors contributing to thermodynamic differences between thermophilic and a mesophilic ribonucleases H.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Investigation of factors contributing to thermodynamic differences between thermophilic and a mesophilic ribonucleases H./
作者:	Robic, Srebrenka.
面頁冊數:	126 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4243.
Contained By:	Dissertation Abstracts International64-09B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3105349
ISBN:	049652916X

Investigation of factors contributing to thermodynamic differences between thermophilic and a mesophilic ribonucleases H.
Robic, Srebrenka.

Investigation of factors contributing to thermodynamic differences between thermophilic and a mesophilic ribonucleases H. - 126 p.

Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4243.

Thesis (Ph.D.)--University of California, Berkeley, 2003.

Ribonucleases H from the thermophilic bacterium Thermus thermophilus and the mesophile Escherichia coli have drastically different thermodynamic profiles. The thermophilic ribonuclease H is more stable at all temperatures and has a broader dependence of thermodynamic stability on temperature, i.e. a significantly lower change in heat capacity upon unfolding (DeltaCp). To determine how the core and periphery regions contribute to the different stability profiles of these two ribonucleases H, I designed and characterized two chimeric proteins. Biophysical studies of the two chimeric ribonucleases H show that the core region is essential for both the increased stability and the lower DeltaCp seen for the thermophilic protein. The low DeltaCp feature is very surprising, and is unexpected based on the same structures of the two homologous proteins. I propose that a novel feature, residual structure in the unfolded state of the thermophilic ribonuclease H, is the origin of this unusually low DeltaCp. This hypothesis is examined by differential scanning calorimetry and by thermodynamic characterization of variants designed to perturb this residual structure. The results of both of these studies are consistent with the residual structure localized to the core region of unfolded T. thermophilus RNase H, and with no residual structure in the unfolded state of the mesophilic homolog from E. coli. Residual structure in the unfolded state of thermophilic proteins may provide a mechanism for balancing a high Tm with a thermodynamic stability optimized for the protein's function and may serve as a general explanation for broader stability curves of a whole class of thermophilic proteins.

ISBN: 049652916XSubjects--Topical Terms:

1019105
Biophysics, General.

Investigation of factors contributing to thermodynamic differences between thermophilic and a mesophilic ribonucleases H.
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502 $a Thesis (Ph.D.)--University of California, Berkeley, 2003.
520 $a Ribonucleases H from the thermophilic bacterium Thermus thermophilus and the mesophile Escherichia coli have drastically different thermodynamic profiles. The thermophilic ribonuclease H is more stable at all temperatures and has a broader dependence of thermodynamic stability on temperature, i.e. a significantly lower change in heat capacity upon unfolding (DeltaCp). To determine how the core and periphery regions contribute to the different stability profiles of these two ribonucleases H, I designed and characterized two chimeric proteins. Biophysical studies of the two chimeric ribonucleases H show that the core region is essential for both the increased stability and the lower DeltaCp seen for the thermophilic protein. The low DeltaCp feature is very surprising, and is unexpected based on the same structures of the two homologous proteins. I propose that a novel feature, residual structure in the unfolded state of the thermophilic ribonuclease H, is the origin of this unusually low DeltaCp. This hypothesis is examined by differential scanning calorimetry and by thermodynamic characterization of variants designed to perturb this residual structure. The results of both of these studies are consistent with the residual structure localized to the core region of unfolded T. thermophilus RNase H, and with no residual structure in the unfolded state of the mesophilic homolog from E. coli. Residual structure in the unfolded state of thermophilic proteins may provide a mechanism for balancing a high Tm with a thermodynamic stability optimized for the protein's function and may serve as a general explanation for broader stability curves of a whole class of thermophilic proteins.
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