Foldable Detergents for Membrane Protein Study: Importance of Detergent Core Flexibility in Protein Stabilization.
Ontology highlight
ABSTRACT: Membrane proteins are of biological and pharmaceutical significance. However, their structural study is extremely challenging mainly due to the fact that only a small number of chemical tools are suitable for stabilizing membrane proteins in solution. Detergents are widely used in membrane protein study, but conventional detergents are generally poor at stabilizing challenging membrane proteins such as G protein-coupled receptors and protein complexes. In the current study, we prepared tandem triazine-based maltosides (TZMs) with two amphiphilic triazine units connected by different diamine linkers, hydrazine (TZM-Hs) and 1,2-ethylenediamine (TZM-Es). These TZMs were consistently superior to a gold standard detergent (DDM) in terms of stabilizing a few membrane proteins. In addition, the T
SUBMITTER: Ghani L
PROVIDER: S-EPMC9007890 | biostudies-literature | 2022 Apr
REPOSITORIES: biostudies-literature
ACCESS DATA