Brielle Esther S, Arkin Isaiah T
The Alexander Silberman Institute of Life Sciences, Department of Biological Chemistry , The Hebrew University of Jerusalem , Edmond J. Safra Campus , Jerusalem 91904 , Israel.
J Phys Chem Lett. 2018 Jul 19;9(14):4059-4065. doi: 10.1021/acs.jpclett.8b01675. Epub 2018 Jul 9.
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.
