Local chemistry of the surfactant's head groups determines protein stability in reverse micelles-Reference-Cited by-同舟云学术

Local chemistry of the surfactant's head groups determines protein stability in reverse micelles

Published:2018 Issue:13 Volume:20 Page:8515-8522
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Senske Michael¹²³⁴,Xu Yao¹²³⁴,Bäumer Alexander¹²³⁴,Schäfer Sarah¹²³⁴,Wirtz Hanna¹²³⁴,Savolainen Janne¹²³⁴,Weingärtner Hermann¹²³⁴,Havenith Martina¹²³⁴^ORCID

Affiliation:

1. Department of Physical Chemistry II

2. Ruhr-Universität Bochum

3. 44780 Bochum

4. Germany

Abstract

Protein stability in reverse micelles is determined by local chemical interactions between the surfactant molecules and the protein groups.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C8CP00407B

Reference64 articles.

1. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

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3. In-cell thermodynamics and a new role for protein surfaces

4. The temperature dependence of the Hofmeister series: thermodynamic fingerprints of cosolute–protein interactions

5. Thermodynamic study of globular protein stability in microemulsions

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