Near-infrared photoacoustic spectroscopy of proteins.
A major problem encountered with the use of electronic spectroscopy in the analysis of biological materials in the ultraviolet, visible, and infrared region involves the limited range of the physical state of samples that can be examined. In an attempt to expand this range, photoacoustic spectra of both solid- and solution-state proteins have been obtained in the near-infrared region. Solid proteins generate detailed spectra in the region 1.0-2.6 micron, resulting primarily from hydrogenic overtone and combinational modes. Harmonics and combinations of amide group frequencies which display significant spectral complexity are observed between 1.4 and 1.7 micron, although they appear to manifest only limited conformational sensitivity. Solution spectra in D2O are of much lower resolution. Assignments of peaks for both solution- and solid-state proteins are presented and the advantages and disadvantages of the use of near-infrared photoacoustic spectroscopy with proteins are discussed.
D000596:Amino Acids / Q000032:analysis; D010455:Peptides / Q000032:analysis; D010777:Photochemistry; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis*; D013055:Spectrophotometry, Infrared / Q000379:methods*
D000596:Amino Acids; D010455:Peptides; D011506:Proteins