Analyzing protein dynamics using hydrogen exchange mass spectrometry
All cellular processes depend on the functionality of proteins. Although the functionality of a given protein is the direct consequence of its unique amino acid sequence, it is only realized by the folding of the polypeptide chain into a single defined three-dimensional arrangement or more commonly...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) Video |
| Sprache: | Englisch |
| Veröffentlicht: |
November 29, 2013
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| In: |
JoVE. Video journal
Year: 2013, Heft: 81 |
| ISSN: | 1940-087X |
| DOI: | 10.3791/50839 |
| Schlagworte: | |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3791/50839 Verlag, lizenzpflichtig, Volltext: https://www.jove.com/v/50839/analyzing-protein-dynamics-using-hydrogen-exchange-mass-spectrometry 
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| Verfasserangaben: | Nikolai Hentze and Matthias P. Mayer |
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| 520 | |a All cellular processes depend on the functionality of proteins. Although the functionality of a given protein is the direct consequence of its unique amino acid sequence, it is only realized by the folding of the polypeptide chain into a single defined three-dimensional arrangement or more commonly into an ensemble of interconverting conformations. Investigating the connection between protein conformation and its function is therefore essential for a complete understanding of how proteins are able to fulfill their great variety of tasks. One possibility to study conformational changes a protein undergoes while progressing through its functional cycle is hydrogen-1H/2H-exchange in combination with high-resolution mass spectrometry (HX-MS). HX-MS is a versatile and robust method that adds a new dimension to structural information obtained by e.g. crystallography. It is used to study protein folding and unfolding, binding of small molecule ligands, protein-protein interactions, conformational changes linked to enzyme catalysis, and allostery. In addition, HX-MS is often used when the amount of protein is very limited or crystallization of the protein is not feasible. Here we provide a general protocol for studying protein dynamics with HX-MS and describe as an example how to reveal the interaction interface of two proteins in a complex. | ||
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