Abstract
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 language | English |
|---|---|
| Pages (from-to) | 394-401 |
| Number of pages | 8 |
| Journal | Current Opinion in Chemical Biology |
| Volume | 10 |
| Issue number | 5 |
| DOIs | |
| State | Published - 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 .