Gaining insight into membrane protein structure using isotope-edited FTIR

Joshua Manor, Isaiah T. Arkin*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

12 Scopus citations


FTIR spectroscopy has long been used as a tool used to gain average structural information on proteins. With the advent of stable isotope editing, FTIR can be used to derive accurate information on isolated amino acids. In particular, in an anisotropic sample such as membrane layers, it is possible to measure the orientation of the peptidic carbonyl groups. Herein, we review the theory that enables one to obtain accurate restraints from FTIR spectroscopy, alongside considerations for sample suitability and general applicability. We also propose approaches that may be used to generate structural models of simple membrane proteins based on FTIR orientational restraints. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.

Original languageAmerican English
Pages (from-to)2256-2264
Number of pages9
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number10
StatePublished - 2013

Bibliographical note

Funding Information:
This work was supported in part by grants from the National Institutes of Health ( R21AI064797 ), the Israeli Science Foundation ( 784/01 , 1249/05 , 1581/08 ) and the Horowitz Foundation . ITA is the Arthur Lejwa Professor of Structural Biochemistry at the Hebrew University of Jerusalem.


  • FTIR
  • Isotope editing
  • Membrane protein
  • Molecular modeling


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