The aggregation behavior of zinc-free insulin studied by small-angle neutron scattering
作者： JanSkov Pedersen , Steen Hansen , Rogert Bauer
DOI: 10.1007/BF00180159
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摘要: The aggregation behavior of zinc-free insulin has been studied by small-angle neutron scattering as a function pH and ionic strength the solution. pair distance distribution functions for 12 samples have obtained indirect Fourier transformation. results show that diameter aggregates is 40 A at 11 10 mM NaCl, independent protein concentration. largest about 120 found 8, 100 concentration mg/ml. Estimates functions, free inter-particle correlation effects, were an transformation, omitting data small vectors, which are influenced these effects. By this procedure weight-averaged molecular mass average radius gyration determined. These parameters vary from 1.3 times monomer 14 A, to 6.8 31 respectively. between oligomers was determined model based on crystal structure insulin. transformations compared equilibrium recently introduced Kadima et al. (1993). agree well with predictions except broader distributions suggested scattering.
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