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Probing serpin conformational change using mass spectrometry and related methods

Tsutsui, Yuko and Sarkar, Anindya and Wintrode, Patrick L. (2011) Probing serpin conformational change using mass spectrometry and related methods. In: Serpin Biology and Therapy. Methods in Enzymology. No.501. Academic Press , Oxford , pp. 325-350. ISBN 9780123859501. https://resolver.caltech.edu/CaltechAUTHORS:20111122-081018125

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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.


Item Type:Book Section
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/B978-0-12-385950-1.00015-8DOIUNSPECIFIED
http://www.sciencedirect.com/science/article/pii/B9780123859501000158PublisherUNSPECIFIED
http://www.ncbi.nlm.nih.gov/pubmed/22078541PubMed CentralUNSPECIFIED
Additional Information:© 2011 Elsevier Inc. Available online 9 November 2011.
Subject Keywords:Hydrogen/deuterium exchange; Mass spectrometry; HXMS; Protein dynamics; Serpin; Protein folding; Misfolding disease
Series Name:Methods in Enzymology
Issue or Number:501
Record Number:CaltechAUTHORS:20111122-081018125
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20111122-081018125
Official Citation:Yuko Tsutsui, Anindya Sarkar, Patrick L. Wintrode, Chapter Fifteen - Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods, In: James C. Whisstock and Phillip I. Bird, Editor(s), Methods in Enzymology, Academic Press, 2011, Volume 501, Pages 325-350, ISSN 0076-6879, ISBN 9780123859501, 10.1016/B978-0-12-385950-1.00015-8.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:27901
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:28 Nov 2011 21:51
Last Modified:03 Oct 2019 03:27

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