Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL.

@article{Taniguchi2004StoppedflowFA,
  title={Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL.},
  author={Masaaki Taniguchi and Tatsunari Yoshimi and Kunihiro Hongo and Tomohiro Mizobata and Yasushi Kawata},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 16},
  pages={16368-76}
}
GroEL undergoes numerous conformational alterations in the course of facilitating the folding of various proteins, and the specific movements of the GroEL apical domain are of particular importance in the molecular mechanism. In order to monitor in detail the numerous movements of the GroEL apical domain, we have constructed a mutant chaperonin (GroEL R231W… CONTINUE READING