Advances in mass spectrometry-based footprinting of membrane proteins

Jie Sun, Weikai Li, Michael L. Gross

Research output: Contribution to journalReview articlepeer-review

1 Scopus citations

Abstract

Structural biology is entering an exciting time where many new high-resolution structures of large complexes and membrane proteins (MPs) are determined regularly. These advances have been driven by over 15 years of technological improvements, first in macromolecular crystallography, and recently in cryo-electron microscopy. Obtaining information about MP higher order structure and interactions is also a frontier, important but challenging owing to their unique properties and the need to choose suitable detergents/lipids for their study. The development of mass spectrometry (MS), both instruments and methodology in the past 10 years, has also advanced it as a complementary method to study MP structure and interactions. In this review, we discuss advances in MS-based footprinting for MPs and highlight recent methodologies that offer new promise for MP study by chemical footprinting and mass spectrometry.

Original languageEnglish
Article number2100222
JournalProteomics
Volume22
Issue number8
DOIs
StatePublished - Apr 2022

Keywords

  • fast photochemical oxidation of proteins
  • hydrogen deuterium exchange
  • irreversible amino acid footprinting
  • protein footprinting

Fingerprint

Dive into the research topics of 'Advances in mass spectrometry-based footprinting of membrane proteins'. Together they form a unique fingerprint.

Cite this