Probing Carbohydrate Product Expulsion from a Processive Cellulase with Multiple Absolute Binding Free Energy Methods*

@inproceedings{Bu2011ProbingCP,
  title={Probing Carbohydrate Product Expulsion from a Processive Cellulase with Multiple Absolute Binding Free Energy Methods*},
  author={Lintao Bu and Gregg T Beckham and Michael R. Shirts and Mark R. Nimlos and William S. Adney and Michael E. Himmel and Michael F. Crowley},
  booktitle={The Journal of biological chemistry},
  year={2011}
}
Understanding the enzymatic mechanism that cellulases employ to degrade cellulose is critical to efforts to efficiently utilize plant biomass as a sustainable energy resource. A key component of cellulase action on cellulose is product inhibition from monosaccharide and disaccharides in the product site of cellulase tunnel. The absolute binding free energy of cellobiose and glucose to the product site of the catalytic tunnel of the Family 7 cellobiohydrolase (Cel7A) of Trichoderma reesei… CONTINUE READING

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Product Expulsion Free Energy of Cel7A 18168 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

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