1989
DOI: 10.1016/0167-4838(89)90121-0
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Conformational transitions in poly(l-lysine): studies using Fourier transform infrared spectroscopy

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Cited by 167 publications
(184 citation statements)
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“…Without carbohydrate, drying led to absorption bands at 1625 and 1695 cm Ϫ1 , which are indicative of extended ␤-sheet structure. In the hydrated state poly-lLys exists entirely in the random coil conformation (Tiffany and Krimm, 1969;Jackson et al, 1989;Wolkers et al, 1998d). The above results show that umbelliferose, similar to Suc, can prevent dehydration-induced conformational transitions of poly-l-Lys.…”
Section: Protein Protectionsupporting
confidence: 49%
“…Without carbohydrate, drying led to absorption bands at 1625 and 1695 cm Ϫ1 , which are indicative of extended ␤-sheet structure. In the hydrated state poly-lLys exists entirely in the random coil conformation (Tiffany and Krimm, 1969;Jackson et al, 1989;Wolkers et al, 1998d). The above results show that umbelliferose, similar to Suc, can prevent dehydration-induced conformational transitions of poly-l-Lys.…”
Section: Protein Protectionsupporting
confidence: 49%
“…An assumption in this type of quantitative analysis is that the molar absorptions of the amide I bands assigned to different conformers are equal. This assumption may not be correct in all cases [46][47][48]. However, other studies reported similar intensities for β-stranded and helical polypeptides [47,49], and comparable absorptions were found for β-stranded and random-coiled structures which were obtained from proteins in aqueous solution [50].…”
Section: Figure 7 Dependence Of Fluorescence Energy Transfer On the Rmentioning
confidence: 82%
“…As demonstrated via Raman spectroscopy, the O-H bending and stretching vibrations of water undergo significant changes in the presence of proteins and other solutes (37,40,41). Increasing evidence also supports the idea that different molar extinction coefficients exist for the various structure types contributing to the protein amide vibrations (33,42,43). Accurate subtraction of background solvent and assignment of the proper weights to the amide band components are critical for obtaining reliable secondary structure estimates, especially in cases involving low protein concentrations.…”
Section: Fourier-transformed Infrared (Ftir)mentioning
confidence: 89%