Estimation of beta-structure content of proteins by means of deconvolved FTIR spectra.
Fourier self-deconvolution was applied to the infrared spectra of five globular proteins with a high beta-structure content and to the essentially alpha-helical protein hemoglobin. The featureless amide I' bands around 1650 cm-1 were thereby resolved into six to nine components, depending on the protein. Specific components were assigned to the beta-structure segments in each protein. The frequencies and the number of 'beta-bands' differ from one protein to another. The areas of the components were evaluated by means of a Gauss-Newton iteration procedure. It appears that the total area of the beta-bands, as a fraction of the total amide I' band area, reflects the relative beta-structure content of each protein studied.
D000577:Amides / Q000032:analysis; D002918:Chymotrypsin / Q000032:analysis; D002919:Chymotrypsinogen / Q000032:analysis; D003208:Concanavalin A / Q000032:analysis; D005583:Fourier Analysis; D006454:Hemoglobins / Q000032:analysis; D011487:Protein Conformation; D012259:Ribonuclease, Pancreatic / Q000032:analysis; D012260:Ribonucleases / Q000032:analysis; D013055:Spectrophotometry, Infrared / Q000379:methods
D000577:Amides; D006454:Hemoglobins; D003208:Concanavalin A; D002919:Chymotrypsinogen; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic; C022542:ribonuclease S; D002918:Chymotrypsin