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The structure and properties of napin-seed storage protein from rape (Brassica napus L.)



The structure and properties of napin-seed storage protein from rape (Brassica napus L.)



Nahrung 42(3/4): 201-204



Purification to homogeneity of 2S albumin storage protein from rape seeds (napin) was achieved and its secondary structure and conformational stability were characterised by circular dichroism (CD) and high-sensitivity differential scanning calorimetry (HS-DSC). Deconvolution of the far-UV CD spectrum of napin revealed about 25% of alpha -helix and 38% of beta -sheet structure at neutral and slightly acid pH.

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Accession: 003315530

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DOI: 10.1002/(sici)1521-3803(199808)42:03/04<201::aid-food201>3.0.co;2-u



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