FTIR studies of secondary structures of bovine insulin and its derivatives

• Published in: Biochimica et biophysica acta Vol. 1080; no. 1; pp. 29 - 33
• Main Authors: Wei, Jiang, Lin, Ying-Zhang, Zhou, Jun-Mei, Tsou, Chen-Lu
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 11.10.1991; Elsevier
• Subjects: Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Cattle; Desoctapeptide insulin; Despentapeptide insulin; FTIR; Fundamental and applied biological sciences. Psychology; Insulin; Insulin - analogs & derivatives; Insulin - chemistry; Peptides - chemistry; Protein Conformation; Proteins; Secondary structure; Spectrophotometry, Infrared; Swine; Desoctapeptide insulin; DTT; FTIR; Despentapeptide insulin; Secondary structure; DPI; Insulin; DOI; Pancreatic hormone; Fourier transformation; Bovine; Infrared spectrometry; C terminal-Sequence; Protein hormone; Vertebrata; Mammalia; Deletion; Artiodactyla; Ungulata
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/0167-4838(91)90107-B

The amide I bands of the deconvolved FTIR spectrum of bovine insulin, despentapeptide(B26-B30) insulin and desoctapeptide(B23-B30) insulin in D 2O solution have been assigned to α-helix, the 3 10 helix, irregular helix, extended chains, β-turns and other secondary structures. From the peak areas the relative contents of these structures obtained are in general agreement with those calculated from the known structures of porcine insulin and DPI in the crystalline state. The main difference in the structure of DOI with those of insulin and DPI is the shortening of the helix segment and an extended chain for the C terminal segment in the B chain.