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Protein stability in mixed solvents: From transfer thermodynamics to the denaturation by urea and back

Moeser, Beate (2016) Protein stability in mixed solvents: From transfer thermodynamics to the denaturation by urea and back. PhD, Universität Regensburg.

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Date of publication of this fulltext: 10 May 2016 05:41

Abstract (English)

The conformational equilibrium between folded and unfolded protein structures is sensitive to the presence of cosolvents in the surrounding solution, and several small organic molecules are known to modulate the functioning of proteins in cells by shifting the equilibrium toward folded (stabilizers) or unfolded states (denaturants). The molecular mechanisms behind these effects are not yet fully ...


Translation of the abstract (German)

Das Konformationsgleichgewicht zwischen gefalteten und ungefalteten Proteinstrukturen wird durch das Vorhandensein von Kosolvenzien in der umgebenden Lösung beeinflusst und einige niedermolekulare organische Moleküle sind dafür bekannt, die Funktionsfähigkeit von Proteinen in Zellen zu modulieren, indem sie das Gleichgewicht in Richtung gefalteter (Stabilisatoren) oder entfalteter Zustände ...


Export bibliographical data

Item type:Thesis of the University of Regensburg (PhD)
Date:10 May 2016
Referee:Prof. Dr. Dominik Horinek
Date of exam:7 May 2015
Institutions:Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry)
Keywords:protein denaturation, urea, cosolvents, cosolutes, transfer free energies, protein stability, mixed solvents, transfer thermodynamics, transfer model, vapor pressure, molecular dynamics, protein folding, concentration scale, activity coefficient
Dewey Decimal Classification:500 Science > 540 Chemistry & allied sciences
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:31912
Owner only: item control page


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