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- W2144001142 abstract "We have measured 〈RH〉z, 〈R〉 Z ½ , and 〈M〉w for individual fractions of the protein α-crystallin obtained by gel filtration of bovine lens nuclear extracts. A strong and monotonic decrease of 〈RH〉z and 〈M〉w with increasing elution volume could be observed, indicating a broad size distribution. The experimental results are quantitatively consistent with a polymerization of monomeric units into linear chains, which may have a certain degree of flexibility. Using theoretical expressions for 〈R〉 and RH originally derived for semiflexible polymers in solution, we can self-consistently analyse the data from static and dynamic light scattering, and from electron microscopy experiments. We thus obtain detailed information on the molecular weight distribution and the quaternary structure of α-crystallin in these solutions." @default.
- W2144001142 created "2016-06-24" @default.
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- W2144001142 date "1991-09-01" @default.
- W2144001142 modified "2023-10-10" @default.
- W2144001142 title "Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine ?-crystallin" @default.
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- W2144001142 doi "https://doi.org/10.1002/bip.360311011" @default.
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