| Autor: |
Justin T. Seffernick, SM Bargeen Alam Turzo, Sophie R. Harvey, Yongseok Kim, Árpád Somogyi, Shir Marciano, Vicki H. Wysocki, Steffen Lindert |
| Rok vydání: |
2023 |
| Předmět: |
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| Zdroj: |
Analytical chemistry. 94(29) |
| ISSN: |
1520-6882 |
| Popis: |
Understanding the relationship between protein structure and experimental data is crucial for utilizing experiments to solve biochemical problems and optimizing the use of sparse experimental data for structural interpretation. Tandem mass spectrometry (MS/MS) can be used with a variety of methods to collect structural data for proteins. One example is surface-induced dissociation (SID), which is used to break apart protein complexes (via a surface collision) into intact subcomplexes and can be performed at multiple laboratory frame SID collision energies. These energy-resolved MS/MS experiments have shown that the profile of the breakages depends on the acceleration energy of the collision. It is possible to extract an appearance energy (AE) from energy-resolved mass spectrometry (ERMS) data, which shows the relative intensity of each type of subcomplex as a function of SID acceleration energy. We previously determined that these AE values for specific interfaces correlated with structural features related to interface strength. In this study, we further examined the structural relationships by developing a method to predict the full ERMS plot from the structure, rather than extracting a single value. First, we noted that for proteins with multiple interface types, we could reproduce the correct shapes of breakdown curves, further confirming previous structural hypotheses. Next, we demonstrated that interface size and energy density (measured using Rosetta) correlated with data derived from the ERMS plot ( |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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