FTIR studies of secondary structures of bovine insulin and its derivatives.
作者： Jiang Wei , Ying-Zhang Lin , Jun-Mei Zhou , Chen-Lu Tsou
DOI: 10.1016/0167-4838(91)90107-B
关键词:
摘要: The amide I bands of the deconvolved FTIR spectrum bovine insulin, despentapeptide(B26-B30) insulin and desoctapeptide(B23-B30) in D 2 O solution have been assigned to α-helix, 3 10 helix, irregular extended chains, β-turns other secondary structures. From peak areas relative contents these structures obtained are general agreement with those calculated from known porcine DPI crystalline state. main difference structure DOI is shortening helix segment an chain for C terminal B chain.
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