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• W2068900809 abstract "The secondary structure of α-crystallin was examined in powder, film, and aqueous solution by different sampling techniques (specular reflectance, direct or KBr pellet transmission and attenuated total reflectance) using microscopic Fourier transform infrared (FT-IR) spectroscopy. The conformation of α-crystallin was quantitatively estimated from the vibrational analysis of amide I band achieved by second-derivative analysis, Fourier self-deconvolution and curve fitting program. The results indicate that all the α-crystallin samples did not show a large different composition in α-helix structure (12.06%–15.95%). Except in aqueous solution or in KBr pellet, the β-turn (32.05%–34.77%), β-sheet (38.22% –%) or random coil (13.98%–14.96%) structures of α-crystallin was, respectively, found to be similar, indicating that α-crystallin in powder and film states exhibited similar IR spectra and secondary structure determined by specular reflectance and transmission techniques. Once the powder or film of α-crystallin sample was compressed into KBr pellet, the β-sheet composition decreased (38.22%→34.39% for powder; 38.94%→33.16% for film) but the β-turn conformation increased (34.77%→40.24% for powder; 32.05%→37.24% for film). However, the composition of α-crystallin in water showed an unique predominance of β-sheet structure with maximum at 1623 cm−1 and revealed the higher composition of β-sheet (55.36%) and random coil (17.56%), but a lower composition of β-turn (13.64%), respectively. This illustrates that α-crystallin showed a markedly different conformation in aqueous solution, as compared to that in powder or film state." @default.
• W2068900809 created "2016-06-24" @default.
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• W2068900809 date "2000-01-18" @default.
• W2068900809 modified "2023-10-18" @default.
• W2068900809 title "INFRARED MICROSPECTROSCOPIC SAMPLING TECHNIQUES TO DETERMINE THE SECONDARY CONFORMATIONS OF α-CRYSTALLIN IN DIFFERENT STATES" @default.
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• W2068900809 doi "https://doi.org/10.1081/ci-100100959" @default.
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