2001
DOI: 10.1007/s003390100984
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Light can transform the secondary structure of silk protein

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Cited by 67 publications
(37 citation statements)
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“…This result suggested that the conformational change of SF occurred from the random coil to the b-sheet structure due to the cross-linking with EDC. The spectral changes agree well with a result reported previously [44].…”
Section: Coating With Edc Cross-linked Sfsupporting
confidence: 83%
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“…This result suggested that the conformational change of SF occurred from the random coil to the b-sheet structure due to the cross-linking with EDC. The spectral changes agree well with a result reported previously [44].…”
Section: Coating With Edc Cross-linked Sfsupporting
confidence: 83%
“…SEM micrographs of theophylline tablets coated with EDC crosslinked SF. position of absorption frequency is quite sensitive to the secondary structure [44]. The vibrational transition bands of CaO stretching (1655 cm K1 , amide I), N-H de-formation and C-N stretching (1540 cm K1 , amide II), and C-N stretching and N-H deformation (1250 cm K1 , amide III) are seen in the figure.…”
Section: Coating With Edc Cross-linked Sfmentioning
confidence: 82%
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“…Band around 1448 cm 1 is assigned as CH 3 modes of alanine. Phenol of tyrosine is at around 1160 cm 1 [6][7][8][9].…”
Section: Atrmentioning
confidence: 99%
“…While the H chain contains the repetitive peptide and is more hydrophobic, the L chain is non-repetitive and more hydrophilic [35]. The secondary structure of SF is the random coil and the anti-parallel β-sheet structure, which is connected to each peptide by a hydrogen bond [36]. The main crystal structure of SF is silk I and II.…”
Section: Fibroinmentioning
confidence: 99%