Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis.

ABSTRACT: The strength and specificity of protein complex formation is crucial for most life processes and is determined by interactions between residues in the binding partners. Double-mutant cycle analysis provides a strategy for studying the energetic coupling between amino acids at the interfaces of such complexes. Here we show that these pairwise interaction energies can be determined from a single high-resolution native mass spectrum by measuring the intensities of the complexes formed by the two wild-type proteins, the complex of each wild-type protein with a mutant protein, and the complex of the two mutant proteins. This native mass spectrometry approach, which obviates the need for error-prone measurements of binding constants, can provide information regarding multiple interactions in a s

SUBMITTER: Sokolovski M 

PROVIDER: S-EPMC5550451 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature