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Efficient Proteins Structure Prediction Model Using Langevin Modelling Springs

This study by Benjamin Jefferys, Lawrence Kelley, and Mike Sternberg introduces a streamlined protein structure prediction model. By simplifying structures through Langevin modelling and analyzing hydrogen bonds, water interactions, and sidechain interactions, this model produces fast and accurate results. The research covers applications beyond protein folding, showcased at 3DSIG/ISMB, enriching the field of structural bioinformatics. The entry features intricate visual reflections of important forces in protein folding within a TIM barrel domain, with acknowledgements to Lawrence Kelley, Mike Sternberg, Alex Herbert, Daniel Chubb, and the Structural Bioinformatics Group led by Richard Jefferys.

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Efficient Proteins Structure Prediction Model Using Langevin Modelling Springs

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  1. a fast and simple model for protein structure prediction Benjamin Jefferys Lawrence Kelley Mike Sternberg

  2. structure simplification

  3. Langevin modelling

  4. Langevin modelling

  5. springs

  6. springs

  7. backbone conformation

  8. hydrogen bonds

  9. hydrogen bonds

  10. water

  11. water

  12. water

  13. sidechain interactions

  14. sidechain interactions

  15. sidechain interactions

  16. results

  17. results

  18. results

  19. results

  20. results

  21. results

  22. results

  23. other applications

  24. 3DSIG/ISMB presence Laptop set today – films and protein art Visual Reflections entry: Deliberately obfuscated visualisation of forces hypothesized to be important for protein folding in a TIM barrel domain acknowledgements Lawrence Kelley and Mike Sternberg Alex Herbert and Daniel Chubb Structural Bioinformatics Group Richard Jefferys

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