2014
DOI: 10.1039/c3ra45522j
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Structural architecture and solubility of native and modified gliadin and glutenin proteins: non-crystalline molecular and atomic organization

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Cited by 55 publications
(131 citation statements)
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References 47 publications
(55 reference statements)
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“…In all cases, the dry sample had a small hump (d1) and a dominant peak (d2), in agreement with previous reports. 25,27 No sharp Bragg peak was observed in any of the samples under any conditions, indicating that the WG structure was amorphous. The real space distances were estimated according to the equation: = 2 / , where q is the length of the reciprocal lattice vector.…”
Section: Resultsmentioning
confidence: 99%
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“…In all cases, the dry sample had a small hump (d1) and a dominant peak (d2), in agreement with previous reports. 25,27 No sharp Bragg peak was observed in any of the samples under any conditions, indicating that the WG structure was amorphous. The real space distances were estimated according to the equation: = 2 / , where q is the length of the reciprocal lattice vector.…”
Section: Resultsmentioning
confidence: 99%
“…Typically, the pristine WG has no regular self-assembled structure, but denatured aggregates can develop at an elevated temperature, especially in the presence of glycerol. 25 Further thermal treatments can even generate hexagonal close-packed nanostructures (HCP) in WG platics. 25,27,28 Besides the plasticizers, additives, such as acids, bases and urea, have been used to improve the processability of WG.…”
Section: Introductionmentioning
confidence: 99%
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“…It is possible to assess the relative amount of α-helices/random coils and -sheets by comparing the relative size of the IR spectrum in the 1645-1660 cm -1 region to that of the 1620-1635 cm -1 region. 13 To begin with, the relative sizes are not large; the curves are relatively flat in the 1620-1660 cm -1 region.…”
Section: Protein Secondary Structurementioning
confidence: 94%