Site-Specific Hydrogen Exchange in a Membrane Environment Analyzed by Infrared Spectroscopy

Esther S. Brielle*, Isaiah T. Arkin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Hydrogen exchange is a powerful method to examine macromolecules. In membrane proteins, exchange can distinguish between solvent-accessible and -inaccessible residues due to shielding by the hydrophobic environment of the lipid bilayer. Herein, rather than examining which residues undergo hydrogen exchange, we employ a protocol that enables the full deuteration of all polar hydrogens in a membrane protein. We then measure the impact of hydrogen exchange on the shift of the amide I vibrational mode of individually labeled sites. The results enable us to correlate polarity with vibrational shifts, thereby providing a powerful tool to examine specific locations within a membrane protein in its native membrane environment.

Original languageAmerican English
Pages (from-to)4059-4065
Number of pages7
JournalJournal of Physical Chemistry Letters
Issue number14
StatePublished - 19 Jul 2018

Bibliographical note

Publisher Copyright:
© 2018 American Chemical Society.


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