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Title: Structure and molecular mobility of soy glycinin in the solid state
Authors: Kealley, CS
Rout, MK
Dezfouli, MR
Strounina, E
Whittaker, AK
Appelqvist, IAM
Lillford, PJ
Gilbert, EP
Gidley, MJ
Keywords: Small angle scattering
Crystal structure
Nuclear magnetic resonance
Fourier transform spectrometers
Issue Date: Oct-2008
Publisher: American Chemical Society
Citation: Kealley, C. S., Rout, M. K., Dezfouli, M. R., Strounina, E., Whittaker, A. K., Appelqvist, I. A. M., Lilliford, P. J., Gilbert, E. P., & Gidley, M. J. (2008). Structure and molecular mobility of soy glycinin in the solid state. Biomacromolecules, 9(10), 2937-2946. doi:10.1021/bm800721d
Abstract: We report a multitechnique study of structural organization and molecular mobility for soy glycinin at a low moisture content (<30% w/w) and relate these to its glass-to-rubber transition. Small-angle X-ray scattering (SAXS), differential scanning calorimetry (DSC), Fourier transform infrared (FTIR) spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy are used to probe structure and mobility on different length and time scales. NMR (similar to 10(-6) to 10(-3) s) reveals transitions at a higher moisture content (> 17%) than DSC or SAXS, which sample for much longer times (similar to 10 to 10(3) s) and where changes are detected at > 13% water content at 20 degrees C. The mobility transitions are accompanied by small changes in unit-cell parameters and IR band intensities and are associated with the enhanced motion of the polypeptide backbone. This study shows how characteristic features of the ordered regions of the protein (probed by SAXS and FTIR) and mobile segments (probed by NMR and DSC) can be separately monitored and integrated within a mobility transformation framework. © 2008, American Chemical Society
Gov't Doc #: 1397
ISSN: 1525-7797
Appears in Collections:Journal Articles

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