A thermodynamic analysis of the sequence-specific binding of RNA by bacteriophage MS2 coat protein.

@article{Johansson1998ATA,
  title={A thermodynamic analysis of the sequence-specific binding of RNA by bacteriophage MS2 coat protein.},
  author={Hans E. Johansson and D Dertinger and K A LeCuyer and Linda S. Behlen and Charles H. Greef and O. C. Uhlenbeck},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 16},
  pages={9244-9}
}
Most mutations in the sequence of the RNA hairpin that specifically binds MS2 coat protein either reduce the binding affinity or have no effect. However, one RNA mutation, a uracil to cytosine change in the loop, has the unusual property of increasing the binding affinity to the protein by nearly 100-fold. Guided by the structure of the protein-RNA complex, we used a series of protein mutations and RNA modifications to evaluate the thermodynamic basis for the improved affinity: The tight… CONTINUE READING

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Johansson et al

  • R. S. Cahn, S. C. Ingold, Prelog, 5 V.Angew.Chem.Int.Ed.Engl., 385–415. Biochemistry
  • Proc. Natl. Acad. Sci. USA 95
  • 1998
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