Single Sequence tutorial
Explore how sequence-encoded biophysical properties vary across a protein.
The selector below chooses a protein from the original TIM-barrel example used by b2btools. It includes natural TIM-barrel proteins, the de novo designed sTIM-11 protein, and OctaV1, which did not fold into the intended barrel.
The plot shows predictions against residue position. Hover over a residue for its values and click prediction names in the legend to show or hide them. These values describe properties the sequence can encode; they do not guarantee a particular folded structure.
Bs
Ch
Ec
Hu
Lm
OctaV1
Pf
Tb
Tm
Vm
Ye
sTIM_11
Reading the predictions
- DynaMine backbone dynamics: values below 0.69 suggest flexibility; values above 0.80 suggest rigidity.
- Conformational propensities: higher helix, sheet, coil, or ppII values indicate a higher local propensity.
- EFoldMine: values above 0.169 identify residues likely to begin folding through local interactions.
- DisoMine: values above 0.5 indicate likely disorder.
Continue with the MSA tutorial to compare a sequence with its homologues, or submit your own sequence from the single-sequence predictors.