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Electrostatic Contributions to the T...

Mosley, Pamela Lynnette.

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Electrostatic Contributions to the Thermodynamics of Ribonuclease P Protein Folding.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Electrostatic Contributions to the Thermodynamics of Ribonuclease P Protein Folding./
Author:	Mosley, Pamela Lynnette.
Description:	161 p.
Notes:	Source: Dissertation Abstracts International, Volume: 77-09(E), Section: B.
Contained By:	Dissertation Abstracts International77-09B(E).
Subject:	Organic chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10103849
ISBN:	9781339673912

Electrostatic Contributions to the Thermodynamics of Ribonuclease P Protein Folding.
Mosley, Pamela Lynnette.

Electrostatic Contributions to the Thermodynamics of Ribonuclease P Protein Folding. - 161 p.

Source: Dissertation Abstracts International, Volume: 77-09(E), Section: B.

Thesis (Ph.D.)--Duke University, 2016.

Electrostatic interactions are of fundamental importance in determining the structure and stability of macromolecules. For example, charge-charge interactions modulate the folding and binding of proteins and influence protein solubility. Electrostatic interactions are highly variable and can be both favorable and unfavorable. The ability to quantify these interactions is challenging but vital to understanding the detailed balance and major roles that they have in different proteins and biological processes. Measuring pKa values of ionizable groups provides a sensitive method for experimentally probing the electrostatic properties of a protein.

ISBN: 9781339673912Subjects--Topical Terms:

523952
Organic chemistry.

Electrostatic Contributions to the Thermodynamics of Ribonuclease P Protein Folding.
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100 1 $a Mosley, Pamela Lynnette. $3 3192732
245 1 0 $a Electrostatic Contributions to the Thermodynamics of Ribonuclease P Protein Folding.
300 $a 161 p.
500 $a Source: Dissertation Abstracts International, Volume: 77-09(E), Section: B.
500 $a Adviser: Terrence G. Oas.
502 $a Thesis (Ph.D.)--Duke University, 2016.
520 $a Electrostatic interactions are of fundamental importance in determining the structure and stability of macromolecules. For example, charge-charge interactions modulate the folding and binding of proteins and influence protein solubility. Electrostatic interactions are highly variable and can be both favorable and unfavorable. The ability to quantify these interactions is challenging but vital to understanding the detailed balance and major roles that they have in different proteins and biological processes. Measuring pKa values of ionizable groups provides a sensitive method for experimentally probing the electrostatic properties of a protein.
520 $a pKa values report the free energy of site-specific proton binding and provide a direct means of studying protein folding and pH-dependent stability. Using a combination of NMR, circular dichroism, and fluorescence spectroscopy along with singular value decomposition, we investigated the contributions of electrostatic interactions to the thermodynamic stability and folding of the protein subunit of Bacillus subtilis ribonuclease P, P protein. Taken together, the results suggest that unfavorable electrostatics alone do not account for the fact that P protein is intrinsically unfolded in the absence of ligand because the pKa differences observed between the folded and unfolded states are small. Presumably, multiple factors encoded in the P protein sequence account for its IUP property, which may play an important role in its function.
590 $a School code: 0066.
650 4 $a Organic chemistry. $3 523952
650 4 $a Biophysics. $3 518360
650 4 $a Molecular chemistry. $3 1071612
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710 2 $a Duke University. $b Chemistry. $3 1064507
773 0 $t Dissertation Abstracts International $g 77-09B(E).
790 $a 0066
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792 $a 2016
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10103849