Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive UHMR
ORGANISM(S): Escherichia Coli (ncbitaxon:562)
SUBMITTER: Michael Marty
PROVIDER: MSV000093064 | MassIVE | Fri Oct 06 14:59:00 BST 2023
REPOSITORIES: MassIVE
Analytical chemistry 20240610 25
Lipids are critical modulators of membrane protein structure and function. However, it is challenging to investigate the thermodynamics of protein-lipid interactions because lipids can simultaneously bind membrane proteins at different sites with different specificities. Here, we developed a native mass spectrometry (MS) approach using single and double mutants to measure the relative energetic contributions of specific residues on Aquaporin Z (AqpZ) toward cardiolipin (CL) binding. We first mut ...[more]