1986
DOI: 10.1042/bj2330025
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Infra-red and Raman spectroscopic studies of enzyme structure and function

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Cited by 36 publications
(21 citation statements)
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“…This may because of the low sensitivity of thiol group in FT-IR due to the high polarizability of sulfur 29 .…”
Section: Resultsmentioning
confidence: 99%
“…This may because of the low sensitivity of thiol group in FT-IR due to the high polarizability of sulfur 29 .…”
Section: Resultsmentioning
confidence: 99%
“…Amide I, this is primarily characterized by carbonyl stretch at 1630–1670 cm −1 and intense. Thus, α‐helix is characterized by 1645–1660 cm −1 , β‐sheet at 1665–1680 cm −1 and random coil at 1660–1670 cm −1 are intense in both IR and Raman . However, the presence of amide II at frequency 1530–1550 cm −1 and amide III (1230 cm −1 ), Raman‐active occur at 1230–1300 cm −1 .…”
Section: Discussionmentioning
confidence: 99%
“…Important clues to the polypeptide structure can be estimated from in-plane vibrational modes of the amide groups [Wharton, 1986]. Amide 1 which is primarily characterised by the carbonyl stretch normally has an intense absorption at 1,630-1,680 cm-1 depending on 2° structure.…”
Section: Spectrum O F Sulphated Glycoproteinmentioning
confidence: 99%
“…Amide 1 which is primarily characterised by the carbonyl stretch normally has an intense absorption at 1,630-1,680 cm-1 depending on 2° structure. Previ ously quoted evidence on polypeptides [Wharton, 1986] indicates that a-helix predominates at 1,645-1,660 cm '1, (3-sheet at 1,665-1,680 and random coil at 1,660-1,670 cm '1. Based on the intense absorption present in the sulphated glycoprotein at a maximum o f 1,660 cm' 1 it seems likely that both random coil and a-helix contribute to the polypeptide structure, al though it is difficult to separate the contribution of (3-sheet and random coil due to the close proximity of their absorption maxima.…”
Section: Spectrum O F Sulphated Glycoproteinmentioning
confidence: 99%
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