Analysis of Native-Like Ions Using Structures for Lossless Ion Manipulations
Samuel J Allen1, Rachel M Eaton1, Matthew F Bush1
1University of Washington , Department of Chemistry, Box 351700, Seattle, Washington 98195-1700, United States.
Analytical Chemistry
|August 31, 2016
Summary
Structures for Lossless Ion Manipulations (SLIM) successfully separated large native-like protein ions up to 145 kDa. This method provides high resolution, expanding structural biology and biopharmaceutical analysis capabilities.
Area of Science:
- Biophysics
- Structural Biology
- Mass Spectrometry
Background:
- Native mass spectrometry provides structural insights into proteins and protein complexes.
- Ion mobility separation enhances structural information but has limitations with large native-like ions.
Purpose of the Study:
- To implement Structures for Lossless Ion Manipulations (SLIM) for native-like protein and protein complex ion analysis.
- To assess the capability of SLIM in separating and characterizing large native-like ions.
Main Methods:
- Utilized SLIM technology for ion mobility separation of native-like ions.
- Analyzed ions ranging from 12 to 145 kDa.
- Determined collision cross section values and apparent resolving power.
Main Results:
- SLIM successfully separated native-like protein and protein complex ions up to 145 kDa.
- Collision cross section values were within 3% of drift cell measurements, indicating structural retention.
- Achieved the highest reported apparent resolving power of 42 for a protein complex native-like ion.
Conclusions:
- SLIM is effective for analyzing large native-like ions, preserving their structures.
- The high resolving power of SLIM opens new avenues for structural biology and biopharmaceutical characterization.
- SLIM technology shows broad adaptability for analyzing native-like ions, supporting diverse applications.
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