title: Protein Stability in Reverse Micelles.
abstract: The N-terminal SH3 domain of the Drosophila signal transduction protein drk was encapsulated in reverse micelles. Both the temperature of maximum stability and the melting temperature decreased on encapsulation. Dissecting the temperature-dependent stability into enthalpic and entropic contributions reveals a stabilizing enthalpic and a destabilizing entropic contribution. These results do not match the expectations of hard-core excluded volume theory, nor can they be wholly explained by interactions between the head groups in the reverse micelle and the test protein. We suggest that geometric constraints imposed by the reverse micelles need to be considered.
authors: Department of Physical Chemistry II, Ruhr-Universität Bochum, 44780, Bochum, Germany.
authors: Michael
authors: M
authors: Senske
authors: Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599-3290, USA.
authors: Austin E
authors: AE
authors: Smith
authors: Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599-3290, USA. gary_pielak@unc.edu.
authors: Gary J
authors: GJ
authors: Pielak
mesh_terms: D008823:Micelles; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry*
chemical_list: D008823:Micelles; D011506:Proteins
keywords: NMR spectroscopy; macromolecular crowding; protein stability; reverse micelles; thermodynamics