Probing Target Search Pathways during Protein–Protein Association by Rational Mutations Based on Paramagnetic Relaxation Enhancement

Authors

  • Tae-Kyung Yu,

    1. WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
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  • Young-Joo Yun,

    1. WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
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  • Ko On Lee,

    1. WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
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  • Prof. Jeong-Yong Suh

    Corresponding author
    1. WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
    • WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
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  • 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.

Abstract

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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.

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