Charge reduction stabilizes intact membrane protein complexes for mass spectrometry.

ABSTRACT: The study of intact soluble protein assemblies by means of mass spectrometry is providing invaluable contributions to structural biology and biochemistry. A recent breakthrough has enabled similar study of membrane protein complexes, following their release from detergent micelles in the gas phase. Careful optimization of mass spectrometry conditions, particularly with respect to energy regimes, is essential for maintaining compact folded states as detergent is removed. However, many of the saccharide detergents widely employed in structural biology can cause unfolding of membrane proteins in the gas phase. Here, we investigate the potential of charge reduction by introducing three membrane protein complexes from saccharide detergents and show how reducing their overall charge enables gene

SUBMITTER: Mehmood S 

PROVIDER: S-EPMC4594752 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature