Vibrational CD of the amide II band in some model polypeptides and proteins.
The amide II vibrational CD (VCD) spectra of poly (L-glutamic acid) and poly (L-lysine) in various conformational forms and those of several proteins in H2O have been measured. Characteristic VCD patterns have been observed in the amide II region due to helix, beta-sheet, and coil conformations in polypeptides. Based on their x-ray crystal structures, the proteins studied have been assigned to six categories. Proteins in the same category give rise to similar amide II VCD. While the protein conformational type is indicated using the amide II VCD, discrimination between types is less characteristic than with the previously studied amide I' VCD in D2O.
Gupta
V P
VP
Department of Chemistry, University of Illinois, Chicago 60680.
Keiderling
T A
TA
D000577:Amides / Q000737:chemistry*; D002942:Circular Dichroism; D003208:Concanavalin A / Q000737:chemistry; D005583:Fourier Analysis; D010206:Papain / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011099:Polyglutamic Acid / Q000737:chemistry; D011107:Polylysine / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared
D000577:Amides; D010455:Peptides; D011506:Proteins; D003208:Concanavalin A; D011107:Polylysine; D011099:Polyglutamic Acid; D010206:Papain