Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.

  title={Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.},
  author={Seema Mittal and Yufeng Cai and Madhavi N. L. Nalam and Daniel N A Bolon and Celia A Schiffer},
  journal={Journal of the American Chemical Society},
  volume={134 9},
Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and infectivity. Studies of protease dynamics suggest that the rearrangement of the hydrophobic core is essential for enzyme activity. Many mutations in the hydrophobic core are also associated with drug resistance and may modulate the core flexibility. To test the role of flexibility in protease activity, pairs of cysteines were introduced at the interfaces of flexible regions remote from the active site… CONTINUE READING


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