Proteins are chiral molecules, and CD has become a standard technique for assessing conformational attributes of proteins as well as peptides. The CD bands of proteins and peptides are found in the same spectral regions as their absorption bands. These bands can be used to monitor changes in secondary structure during a structural transition. The near-UV spectrum provides a fingerprint of the correctly folded conformation of a protein that is surpassed in sensitivity only by NMR spectroscopy. The BIF has an Aviv 62A DS Circular Dichroism Spectrometer .
Spectrometer reports on transitions between the vibrational energy levels of molecules.
The application of modern spectral deconvolution techniques and isotope labeling methods allows the vibrations of individual functional groups to be resolved and assigned. Because FTIR can be used to study proteins in optically turbid media, it is well-suited to the study of protein assemblies. And, FTIR spectroscopy can resolve individual conformational isomers that interconvert on the picosecond timescale. These attributes make FTIR spectra an ideal complement to CD spectra. The BIF has a Mattson Infinity FTIR Spectrometer .