Computational Protein Stabilization

Levitate automates a set of Rosetta protein design software protocols as an easty-to-use, SaaS offering proven to reliably identify stabilizing mutations in a wide variety of proteins:

  • Correctly predict stabilizing single point mutants
  • Category-leading performance in quantitatively calculating energy change upon point mutation
  • Experimentally proven protein stabilization algorithms

Heighest prediction accuracy and confidence

Only Cyrus delivers software that is refined and tested on large experimental data sets. Our protein mutational free energy predictor has been tested and developed for several years, outperforming similar tools 1.

Experimentally demonstrated thermo-stabilization

Thermo-stabilization is often achieved by re-designing a protein core. Our custom-built stabilization protocol has been experimentally validated on a number of proteins 2.

Category-leading performance

Proven success in predicting free energy change upon mutation for a set of roughly 2000 point mutants, with better accuracy and confidence than any other software 1 X/Y scatter plot. X axis is the number of DDG mutations, and Y axis is the correlation of calculated DDG to experimental DDG.  Rosetta is the highest with a ~0.62 correlation for ~1800 mutations.  Also plotted are EGAD, CC/PBSA and FoldX

Experimentally demonstrated thermo-stabilization

  • Algorithm to predict stabilizing protein core mutations 2
  • Aggressive in silico core re-sampling discovers mutations verified experimentally to stabilize proteins.

Cartoon diagram depicting mutated residues

  1. Kellogg et al. “Role of conformational sampling in computing mutation-induced changes in protein structure and stability.” Proteins 79, 830-838 (2010)  2

  2. Borgo. et al. ”Automated selection of stabilizing mutations in designed and natural proteins”. PNAS 109, 1494-1499 (2012).  2

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