Isotope-edited IR spectroscopy for the study of membrane proteins

Isaiah T. Arkin*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

68 Scopus citations


Fourier transform infrared (FTIR) spectroscopy has long been a powerful tool for structural analysis of membrane proteins. However, because of difficulties in resolving contributions from individual residues, most of the derived measurements tend to yield average properties for the system under study. Isotope editing, through its ability to resolve individual vibrations, establishes FTIR as a method that is capable of yielding accurate structural data on individual sites in a protein.

Original languageAmerican English
Pages (from-to)394-401
Number of pages8
JournalCurrent Opinion in Chemical Biology
Issue number5
StatePublished - Oct 2006

Bibliographical note

Funding Information:
Work in the author's laboratory was supported in part by grants from the Israel Science Foundation (784/01), DFG and the NIH (1R21AI064797-01). I thank MT Zanni, E Bennett and E Arbely for helpful comments on the manuscript and MT Zanni and P Mukherjee for Figure 4 .


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