Remarkably Fast Coupled Folding and Binding of the Intrinsically Disordered Transactivation Domain of cMyb to CBP KIX

@inproceedings{Shammas2013RemarkablyFC,
  title={Remarkably Fast Coupled Folding and Binding of the
Intrinsically Disordered Transactivation Domain of cMyb to CBP KIX},
  author={Sarah L. Shammas and Alexandra J. Travis and Jane Clarke},
  booktitle={The journal of physical chemistry. B},
  year={2013}
}
Association rates for interactions between folded proteins have been investigated extensively, allowing the development of computational and theoretical prediction methods. Less is known about association rates for complexes where one or more partner is initially disordered, despite much speculation about how they may compare to those for folded proteins. We have attached a fluorophore to the N-terminus of the 25 amino acid cMyb peptide used previously in NMR and equilibrium studies (termed… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-10 of 60 references

Rate theories for biologists.

Quarterly reviews of biophysics • 2010

Conformational selection or induced fit: a flux description of reaction mechanism.

Proceedings of the National Academy of Sciences of the United States of America • 2009

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