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- Okuda, Eiko, et al. Show all 8 Authors
- Journal of agricultural and food chemistry 2003 v.51 no.16 pp. 4633-4639
- X-ray diffraction; crystal structure; differential scanning calorimetry; digestion; disulfide bonds; globulins; glycinin; mutants; mutation; seed storage; seeds; soybeans; thermal stability
- ... The constituent subunits of seed storage protein 11S globulin have two disulfide bonds that are common among 11S globulins from legume and nonlegume seeds. In the case of the A1aB1b subunit of soybean 11S globulin, glycinin, Cys12−Cys45 and Cys88−Cys298 are observed by X-ray crystallography. The significance of these two disulfide bonds for structural stability was investigated by mutagenesis of C ...
- Okuda, Eiko, et al. Show all 10 Authors
- European journal of biochemistry 2001 v.268 no.12 pp. 3595-3604
- X-ray diffraction; beta-conglycinin; crystal structure; crystals; models; phaseolin; polysaccharides; soybeans; vicilin
- ... The crystal structures of recombinant and native β homotrimers of soybean β‐conglycinin were determined by X‐ray crystallography at 2.7 and 2.8 Å resolutions, respectively. The crystals of the recombinant and native β homotrimers belong to space group P21 with cell parameters a = 80.51 Å, b = 63.48 Å, c = 131.43 Å, and β = 90.01° and with cell parameters a = 82.78 Å, b = 69.47 Å, c = 125.33 Å and ...