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- W2091738302 abstract "The structure of alpha-crustacyanin, the blue carotenoprotein of lobster (Homarus gammarus) carapace, has been investigated for the first time using small-angle X-ray scattering. In this paper, we have determined the dimensions of this protein composed of eight heterodimeric subunits of beta-crustacyanin. Analysis of the scattering spectra and estimation of the shape of alpha-crustacyanin show that the protein fits into a cylinder with an axial length of 238 A and a radius of 47.5 A, in which the eight beta-crustacyanin molecules are probably arranged in a helical manner." @default.
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- W2091738302 date "2003-05-15" @default.
- W2091738302 modified "2023-10-14" @default.
- W2091738302 title "Quaternary structure of alpha-crustacyanin from lobster as seen by small-angle X-ray scattering" @default.
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- W2091738302 doi "https://doi.org/10.1016/s0014-5793(03)00486-1" @default.
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