FTIR studies of secondary structures of bovine insulin and its derivatives
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...
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Published in | Biochimica et biophysica acta Vol. 1080; no. 1; pp. 29 - 33 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
11.10.1991
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0167-4838 0006-3002 1879-2588 |
DOI: | 10.1016/0167-4838(91)90107-B |