Energy Resolved Mass Spectrometry Data from Surfaced Induced Dissociation Improves Prediction of Protein Complex Structure.

ABSTRACT: Native Mass Spectrometry (nMS) is a versatile technique for elucidating protein structure. Surface-Induced Dissociation (SID) is an activation method in tandem MS predominantly employed for determining protein complex stoichiometry alongside information about interface strengths. SID-nMS data can be collected over a range of acceleration energies, yielding Energy Resolved Mass Spectrometry (ERMS) data. Previous work demonstrated that the onset and appearance energy from SID-nMS can be used in integrative computational and experimental modeling to guide multimeric structure determination in some cases. However, the appearance energy is a single data point, while the ERMS data provide a full pattern of interface breakage. We hypothesized that incorporation of ERMS data into multimeric protei

SUBMITTER: Bolz RM 

PROVIDER: S-EPMC12085879 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature