Probing serpin conformational change using mass spectrometry and related methods
- Others:
- Whisstock, James C.
- Bird, Phillip I.
Abstract
The folding, misfolding, and inhibitory mechanisms of serpins are linked to both thermodynamic metastability and conformational flexibility. Characterizing the structural distribution of stability and flexibility in serpins in solution is challenging due to their large size and propensity for aggregation. Structural mass spectrometry techniques offer powerful tools for probing the mechanisms of serpin function and disfunction. In this chapter, we review the principles of the two most commonly employed structural mass spectrometry techniques-hydrogen/deuterium exchange and chemical footprinting-and describe their application to studying serpin flexibility, stability, and conformational change in solution. We also review the application of both hydrogen/deuterium exchange and ion mobility mass spectrometry to probe the mechanism of serpin polymerization and the structure of serpin polymers.
Additional Information
© 2011 Elsevier Inc. Available online 9 November 2011.Additional details
- Eprint ID
- 27901
- DOI
- 10.1016/B978-0-12-385950-1.00015-8
- Resolver ID
- CaltechAUTHORS:20111122-081018125
- Created
-
2011-11-28Created from EPrint's datestamp field
- Updated
-
2023-06-02Created from EPrint's last_modified field
- Series Name
- Methods in Enzymology
- Series Volume or Issue Number
- 501