A Guide to Differential Scanning Calorimetry of Membrane and Soluble Proteins in Detergents

Methods in Enzymology
Zhengrong Yang, Christie G Brouillette

Abstract

Differential scanning calorimetry (DSC) detects protein thermal unfolding by directly measuring the heat absorbed. Simple DSC experiments that require relatively small amounts of pure material can provide a wealth of information related to structure, especially with respect to domain architecture, without the need for a complete thermodynamic analysis. Thus, DSC is an ideal additional tool for membrane protein characterization and also offers several advantages over indirect thermal unfolding methods. Integral membrane proteins (IMPs) that comprise both large multitopic transmembrane domains (TMDs) and extramembranous domains (EMDs) are differentially affected by detergent interactions with both domains. In fact, in some cases, destabilization of the EMD by detergent may dominate overall IMP stability. This chapter will (1) provide a perspective on the advantages of DSC for membrane protein characterization and stability measurements, including numerous examples spanning decades of research; (2) introduce models for the interaction and destabilization of IMPs by detergents; (3) discuss two case studies from the authors' lab; and (4) offer practical advice for performing DSC in the presence of detergents.

Citations

Jun 13, 2017·Chembiochem : a European Journal of Chemical Biology·Katharina VeithHenning Tidow
Sep 8, 2018·Plant & Cell Physiology·Kristen Van GelderTariq A Akhtar
Sep 27, 2018·The Journal of Physical Chemistry. B·Aaron J WolfeLiviu Movileanu
Oct 17, 2017·The Journal of Physical Chemistry. B·Aaron J WolfeLiviu Movileanu
Mar 30, 2018·The Journal of Physical Chemistry Letters·Aaron J WolfeLiviu Movileanu
Oct 14, 2021·Biochemical Society Transactions·Stephanie A NestorowVerna Frasca

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