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- W2051268817 abstract "The behavior of Escherichia coli 50S ribosomal subunit proteins L7/L12 has been investigated in ribosome reconstitution buffer, TMK buffer, by sedimentation equilibrium and analytical gel filtration. Contrary to previous reports that L7/L12 exists in solution solely as dimer species [Möller, W., Groene, A., Terhorst, C., & Amons, R. (1972) Eur J. Biochem. 25, 5], results presented here indicate that L7/L12 undergoes a monomer-dimer-tetramer self-association, with equal equilibrium constants of 3.5 x 10(4) M-1 obtained for the monomer-dimer and dimer-tetramer steps. These results yield standard Gibbs' free energies of -6.1 +/ 0.6 kcal/mol at 20 degrees C. The observed absence of temperature dependence of this interaction over the range 5-25 degrees C indicated a zero standard enthalpy of self-association. Gel filtration results are presented that confirm the highly elongated shape of the L7/L12 molecule. The data suggest the corresponding Stokes radii for the monomer, dimer, and tetramer are 21-23, 26-28, and 29-32 omicron A, respectively. The significance of these results is discussed." @default.
- W2051268817 created "2016-06-24" @default.
- W2051268817 creator A5000987315 @default.
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- W2051268817 date "1981-08-01" @default.
- W2051268817 modified "2023-09-27" @default.
- W2051268817 title "Solution behavior of proteins L7/L12 from the 50S ribosomal subunit of Escherichia coli" @default.
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- W2051268817 doi "https://doi.org/10.1021/bi00519a019" @default.
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