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Protein structure, stability and dyn...

Smith, Austin E.

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Protein structure, stability and dynamics in cells and cell-like environments.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Protein structure, stability and dynamics in cells and cell-like environments./
作者:	Smith, Austin E.
面頁冊數:	165 p.
附註:	Source: Dissertation Abstracts International, Volume: 77-01(E), Section: B.
Contained By:	Dissertation Abstracts International77-01B(E).
標題:	Chemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3719892
ISBN:	9781339005546

Protein structure, stability and dynamics in cells and cell-like environments.
Smith, Austin E.

Protein structure, stability and dynamics in cells and cell-like environments. - 165 p.

Source: Dissertation Abstracts International, Volume: 77-01(E), Section: B.

Thesis (Ph.D.)--The University of North Carolina at Chapel Hill, 2015.

The intracellular milieu is filled with small molecules, nucleic acids, lipids and proteins. Theories have attempted to explain how macromolecules react to this environment for over 30 years. Recent experiment-based studies have shown that protein stability and dynamics are altered in this environment. I used the loop of chymotrypsin inhibitor 2 and two unfolded proteins (alpha-synuclein and FlgM) to show that the crowded cellular matrix does not necessarily cause structuring of these dynamic regions. Most importantly, I have shown the thermodynamic and mechanistic basis for how protein stability is changed in the cellular environment. To do this I use a marginally stable globular protein (an isolated SH3 domain) to measure stability, dynamics, and folding rates in cells and cell-like environments. Proteins are enthalpically destabilized in cells. The destabilization arises from charge-charge interactions of the cellular environment with the unfolded ensemble of the protein. These interactions also slow folding of the protein. This work will allow creation of a more complete picture of protein thermodynamics inside the cell. Furthermore, the SH3 domain is amenable to studying in vitro protein stability over a broad range of pH values, and allows acquisition of folding and unfolding rates with a variety of crowders. Future efforts will facilitate a better understanding of surface charge interactions and will allow elucidation of a crowder's interaction with the transition state.

ISBN: 9781339005546Subjects--Topical Terms:

516420
Chemistry.

Protein structure, stability and dynamics in cells and cell-like environments.
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