Symmetrical Gas-Phase Dissociation of Noncovalent Protein Complexes via Surface Collisions

Citations Over TimeTop 11% of 2006 papers

Abstract

Previous gas-phase dissociation experiments of protein-protein complexes have resulted in product ion distributions that are asymmetric by charge and mass, providing limited insight into the chemical nature of subunit organization and interaction. In these experiments, a symmetric charge distribution results from an "energy sudden" collision of protein-protein complexes with a surface, indicating that it may be possible to probe the suboligomeric structure of noncovalent complexes in the gas phase. It is proposed that energy sudden surface activation of cytochrome C homodimers results in dissociation without significant unfolding of one of the monomeric subunits. Previously proposed mechanisms for the dissociation of protein-protein complexes are discussed in the context of these results. These experiments demonstrate the potential to preserve the structural details of subunit interaction within a protein-protein complex and help elucidate the asymmetric nature of macromolecular dissociation in the gas phase.

Related Papers

• → Protein painting reveals solvent-excluded drug targets hidden within native protein–protein interfaces(2014)64 cited
• → A molecular interaction field describing nonconventional intermolecular interactions and its application to protein–ligand interaction prediction(2019)21 cited
• → Unique Physicochemical Patterns of Residues in Protein–Protein Interfaces(2018)9 cited
• → DARC: Mapping Surface Topography by Ray-Casting for Effective Virtual Screening at Protein Interaction Sites(2015)23 cited
• → Quantitative comparison of protein-protein interaction interface using physicochemical feature-based descriptors of surface patches(2023)4 cited