Step toward Probing the Nonannular Belt of Membrane Proteins.

ABSTRACT: Integral membrane proteins are embedded in the biological membrane, where they carry out numerous biological processes. Although lipids present in the membrane are crucial for membrane protein function, it remains difficult to characterize many lipid binding events to membrane proteins, such as those that form the annular belt. Here, we use native mass spectrometry along with the charge-reducing properties of trimethylamine N-oxide (TMAO) to characterize a large number of lipid binding events to the bacterial ammonia channel (AmtB). In the absence of TMAO, significant peak overlap between neighboring charge states is observed, resulting in erroneous abundances for different molecular species. With the addition of TMAO, the weighted average charge state (Z_avg) was d

SUBMITTER: Kumar S 

PROVIDER: S-EPMC10355277 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature