Isotope-edited IR spectroscopy for the study of membrane proteins.
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.
Arkin
Isaiah T
IT
The Alexander Silberman Institute of Life Sciences, Department of Biological Chemistry, The Hebrew University of Jerusalem, Edmund J Safra Campus, Givat-Ram, Jerusalem, Israel. arkin@cc.huji.ac.il
D002247:Carbon Isotopes; D008565:Membrane Proteins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D010103:Oxygen Isotopes; D012680:Sensitivity and Specificity; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods
D002247:Carbon Isotopes; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D010103:Oxygen Isotopes