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American Chemical Society, Biomacromolecules, 10(9), p. 2937-2946, 2008

DOI: 10.1021/bm800721d

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Structure and molecular mobility of soy glycinin in the solid state.

Journal article published in 2008 by Cs Kealley, Mk Rout, Mr Dezfouli, Ekaterina Strounina, Ak Whittaker, Iam Appelqvist, Pj Lillford, Ep Gilbert ORCID, Mj Gidley
This paper was not found in any repository; the policy of its publisher is unknown or unclear.
This paper was not found in any repository; the policy of its publisher is unknown or unclear.

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Abstract

We report a multitechnique study of structural organization and molecular mobility for soy glycinin at a low 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