Please use this identifier to cite or link to this item: https://apo.ansto.gov.au/dspace/handle/10238/1712
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dc.contributor.authorKealley, CSen_AU
dc.contributor.authorRout, MKen_AU
dc.contributor.authorDezfouli, MRen_AU
dc.contributor.authorStrounina, Een_AU
dc.contributor.authorWhittaker, AKen_AU
dc.contributor.authorAppelqvist, IAMen_AU
dc.contributor.authorLillford, PJen_AU
dc.contributor.authorGilbert, EPen_AU
dc.contributor.authorGidley, MJen_AU
dc.date.accessioned2009-08-24T04:39:33Zen_AU
dc.date.accessioned2010-04-30T05:06:12Z-
dc.date.available2009-08-24T04:39:33Zen_AU
dc.date.available2010-04-30T05:06:12Z-
dc.date.issued2008-10en_AU
dc.identifier.citationKealley, 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/bm800721den_AU
dc.identifier.govdoc1397-
dc.identifier.issn1525-7797en_AU
dc.identifier.urihttp://dx.doi.org/10.1021/bm800721den_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1712en_AU
dc.description.abstractWe 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 Societyen_AU
dc.language.isoenen_AU
dc.publisherAmerican Chemical Societyen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectCrystal structureen_AU
dc.subjectSoybeansen_AU
dc.subjectNuclear magnetic resonanceen_AU
dc.subjectGlobulinsen_AU
dc.subjectFourier transform spectrometersen_AU
dc.titleStructure and molecular mobility of soy glycinin in the solid state.en_AU
dc.typeJournal Articleen_AU
dc.date.statistics2008-10en_AU
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