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Article

Probing serpin conformational change using mass spectrometry and related methods.

Methods in enzymology - 1 Jan 2011

Tsutsui Yuko, Sarkar Anindya, Wintrode Patrick L

Abstract excerpt

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...

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PMID: 22078541
DOI: 10.1016/B978-0-12-385950-1.00015-8
PMCID: PMC3679668

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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