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Studies of the translational entropy...

Billings, Erik Antonio.

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Studies of the translational entropy contribution to protein stability by use of the HIV-1 protease as a model system.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Studies of the translational entropy contribution to protein stability by use of the HIV-1 protease as a model system./
Author:	Billings, Erik Antonio.
Description:	94 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-01, Section: B, page: 0290.
Contained By:	Dissertation Abstracts International71-01B.
Subject:	Biology, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3395666
ISBN:	9781109585421

Studies of the translational entropy contribution to protein stability by use of the HIV-1 protease as a model system.
Billings, Erik Antonio.

Studies of the translational entropy contribution to protein stability by use of the HIV-1 protease as a model system. - 94 p.

Source: Dissertation Abstracts International, Volume: 71-01, Section: B, page: 0290.

Thesis (Ph.D.)--The Johns Hopkins University, 2009.

In the quest to predict the Gibbs energy of protein stability, the magnitude of the translational entropy contribution to the stability of 2-state oligomeric proteins has yet to be agreed upon by any meaningful consensus of the various research groups engaged in the task. In an effort to resolve the ongoing dispute, the work herein describes the use of the HIV-1 protease as a model system with which to quantitatively compare and contrast the translational entropy contribution predicted by the cratic and Sackur-Tetrode methodologies versus the experimentally observed value. Toward this end, Differential Scanning Calorimetry was used to measure the stability of wild-type dimeric HIV-1 protease and a series of tethered HIV-1 proteases. The difference in stability and total entropy of unfolding is shown to agree within 0.6 +/- 2.0 cal K -1 mol-1 of that which is predicted by the cratic methodology for the reversible 2-state unfolding of a dimeric protein.

ISBN: 9781109585421Subjects--Topical Terms:

1018625
Biology, General.

Studies of the translational entropy contribution to protein stability by use of the HIV-1 protease as a model system.
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040 $a UMI $c UMI
100 1 $a Billings, Erik Antonio. $3 1674278
245 1 0 $a Studies of the translational entropy contribution to protein stability by use of the HIV-1 protease as a model system.
300 $a 94 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-01, Section: B, page: 0290.
500 $a Advisers: Ernesto Freire; Mario Amzel.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2009.
520 $a In the quest to predict the Gibbs energy of protein stability, the magnitude of the translational entropy contribution to the stability of 2-state oligomeric proteins has yet to be agreed upon by any meaningful consensus of the various research groups engaged in the task. In an effort to resolve the ongoing dispute, the work herein describes the use of the HIV-1 protease as a model system with which to quantitatively compare and contrast the translational entropy contribution predicted by the cratic and Sackur-Tetrode methodologies versus the experimentally observed value. Toward this end, Differential Scanning Calorimetry was used to measure the stability of wild-type dimeric HIV-1 protease and a series of tethered HIV-1 proteases. The difference in stability and total entropy of unfolding is shown to agree within 0.6 +/- 2.0 cal K -1 mol-1 of that which is predicted by the cratic methodology for the reversible 2-state unfolding of a dimeric protein.
590 $a School code: 0098.
650 4 $a Biology, General. $3 1018625
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0306
690 $a 0487
690 $a 0786
710 2 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 71-01B.
790 1 0 $a Freire, Ernesto, $e advisor
790 1 0 $a Amzel, Mario, $e advisor
790 $a 0098
791 $a Ph.D.
792 $a 2009
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3395666