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)
    Search for more papers by this author
  • Young-Joo Yun,

    1. WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
    Search for more papers by this author
  • Ko On Lee,

    1. WCU Biomodulation Major, Department of Agricultural, Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)
    Search for more papers by this author
  • 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)
    Search for more papers by this author

  • 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

original image

Keine Zufallsbekanntschaften: Die Assoziation von Proteinen verläuft über kurzlebige Stoßkomplexe, die je nach ihrer Rolle bei der Bildung des spezifischen Komplexes produktiv oder unproduktiv sein können (siehe Schema). Eine Untersuchung der NMR-spektroskopischen paramagnetischen Relaxationsverstärkung von komplexierenden Proteinmutanten zeigt, dass produktive Stoßkomplexe direkt beobachtbar und quantitativ lokalisierbar sind.

Ancillary