This work was supported by the World Class University program (R31-10056), and by a National Research Foundation of Korea (NRF) grant funded by the Ministry of Education, Science and Technology (2011-0025901 and 2010-0025883). We thank the high-field NMR facility at Korea Basic Science Institute for NMR experiments.
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Communication
Probing Target Search Pathways during Protein–Protein Association by Rational Mutations Based on Paramagnetic Relaxation Enhancement†
Article first published online: 12 FEB 2013
DOI: 10.1002/anie.201208688
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Yu, T.-K., Yun, Y.-J., Lee, K. O. and Suh, J.-Y. (2013), Probing Target Search Pathways during Protein–Protein Association by Rational Mutations Based on Paramagnetic Relaxation Enhancement . Angew. Chem. Int. Ed., 52: 3384–3388. doi: 10.1002/anie.201208688
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Publication History
- Issue published online: 13 MAR 2013
- Article first published online: 12 FEB 2013
- Manuscript Revised: 27 DEC 2012
- Manuscript Received: 30 OCT 2012
Funded by
- World Class University program. Grant Number: R31-10056
- National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology. Grant Numbers: 2011-0025901, 2010-0025883
Keywords:
- encounter complexes;
- equilibrium binding;
- NMR spectroscopy;
- paramagnetic relaxation enhancements;
- protein-protein interactions
Not just a random encounter: Protein–protein association involves short-lived encounter complexes that can be productive or non-productive according to their roles in the specific complex formation (see scheme). A study of mutant proteins forming a complex based on NMR paramagnetic relaxation enhancement demonstrates that productive encounter complexes can be directly monitored and located quantitatively.