Subsecond Time-Resolved Mass Spectrometry in Dynamic Structural Biology
| Autor: | Derek J. Wilson, Cristina Lento |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Resolution (mass spectrometry) Protein Conformation Biomolecule Cryoelectron Microscopy Proteins Nanotechnology General Chemistry 010402 general chemistry Mass spectrometry 01 natural sciences Mass Spectrometry 0104 chemical sciences Folding (chemistry) 03 medical and health sciences Structural biology chemistry Biology Flux (metabolism) Time-resolved mass spectrometry 030304 developmental biology Macromolecule |
| Zdroj: | Chemical Reviews. 122:7624-7646 |
| ISSN: | 1520-6890 0009-2665 |
| Popis: | Life at the molecular level is a dynamic world, where the key players─proteins, oligonucleotides, lipids, and carbohydrates─are in a perpetual state of structural flux, shifting rapidly between local minima on their conformational free energy landscapes. The techniques of classical structural biology, X-ray crystallography, structural NMR, and cryo-electron microscopy (cryo-EM), while capable of extraordinary structural resolution, are innately ill-suited to characterize biomolecules in their dynamically active states. Subsecond time-resolved mass spectrometry (MS) provides a unique window into the dynamic world of biological macromolecules, offering the capacity to directly monitor biochemical processes and conformational shifts with a structural dimension provided by the electrospray charge-state distribution, ion mobility, covalent labeling, or hydrogen-deuterium exchange. Over the past two decades, this suite of techniques has provided important insights into the inherently dynamic processes that drive function and pathogenesis in biological macromolecules, including (mis)folding, complexation, aggregation, ligand binding, and enzyme catalysis, among others. This Review provides a comprehensive account of subsecond time-resolved MS and the advances it has enabled in dynamic structural biology, with an emphasis on insights into the dynamic drivers of protein function. |
| Databáze: | OpenAIRE |
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