Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool

Area of Science:

• Structural Biology
• Biochemistry
• Analytical Chemistry

Background:

• Native mass spectrometry (nMS) is increasingly vital for determining protein structures.
• Advancements in separation, ionization, and hybrid ion mobility-mass spectrometry systems enhance nMS capabilities.
• Novel activation methods are crucial for dissociating protein complexes to reveal structural details.

Purpose of the Study:

• To review the advantages of surface-induced dissociation (SID) for analyzing protein and nucleoprotein complexes.
• To highlight SID's role in elucidating protein structure, particularly when combined with cryo-electron microscopy (cryo-EM) and computational modeling.
• To showcase the utility of nMS and SID in structural biology through case studies.

Main Methods:

• Utilizing native mass spectrometry (nMS) with various preparation and ionization techniques.
• Employing surface-induced dissociation (SID) for controlled fragmentation of protein complexes.
• Integrating nMS/SID data with complementary structural biology methods like cryo-EM and computational modeling.

Main Results:

• SID effectively probes subunit connectivity in protein and nucleoprotein assemblies.
• SID data aligns with structures determined by X-ray crystallography and cryo-EM.
• nMS and SID provide structural insights inaccessible to traditional methods.

Conclusions:

• Surface-induced dissociation (SID) is a key technique for structural elucidation within native mass spectrometry (nMS).
• The integration of nMS/SID with cryo-EM and computational modeling offers powerful approaches for understanding complex biological assemblies.
• Wider adoption of nMS and SID technologies will significantly advance future structural biology research.