Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in alpha-, beta-, and random coil conformations.
Infrared spectra of poly(D,L-alanine), poly(L-glutamic acid), poly(L-lysine), silk fibroin, and tropomyosin have been registered for various conformations of the polypeptide chain. Assuming additivity of the main- and side-chain absorption, spectral parameters of amide I and II absorption bands corresponding to alpha-, beta-, and random coil conformations have been derived. The amide I band parameters for H2O and D2O have been compared.
Venyaminov SYu
Institute of Protein Research, Academy of Sciences of the USSR, Puschino, Moscow Region.
Kalnin
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D000577:Amides / Q000737:chemistry*; D000818:Animals; D002942:Circular Dichroism; D005349:Fibroins / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011099:Polyglutamic Acid / Q000737:chemistry; D011107:Polylysine / Q000737:chemistry; D011487:Protein Conformation; D011817:Rabbits; D013055:Spectrophotometry, Infrared; D014335:Tropomyosin / Q000737:chemistry; D014867:Water
D000577:Amides; D010455:Peptides; D014335:Tropomyosin; D014867:Water; D011107:Polylysine; C019529:polyalanine; D011099:Polyglutamic Acid; D005349:Fibroins