Interactions causing the kinetic trap in serpin protein folding.

@article{Im2002InteractionsCT,
  title={Interactions causing the kinetic trap in serpin protein folding.},
  author={Hana Im and Mi-Sook Woo and Kwang Yeon Hwang and Myeong-Hee Yu},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 48},
  pages={46347-54}
}
Conformational transition is fundamental to the mechanism of functional regulation in proteins, and serpins (serine protease inhibitors) can provide insight into this process. Serpins are metastable in their native forms, and they ordinarily undergo conformational transition to a stable state only when they form a tight complex with target proteases. The metastable native form is thus considered to be a kinetically trapped folding intermediate. We sought to understand the nature of the serpin… CONTINUE READING
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