Welcome to DynaMine!

DynaMine is a fast predictor of protein backbone dynamics using only sequence information as input. Given a protein sequence, DynaMine predicts backbone flexibility at the residue-level in the form of backbone N-H S² order parameter values. These S² values represent how restricted the movement of the atomic bond vector is with respect to the molecular reference frame. A value of 1 means complete order (stable conformation), while a value of 0 means fully random bond vector movement (highly dynamic).
DynaMine has been trained on backbone N-H S² order parameter values that have been directly estimated from experimentally determined NMR chemical shifts. Although it is based on a simple linear regression approach, DynaMine is able to accurately distinguish regions of different structural organization within proteins, such as folded domains and disordered linkers of different sizes. Additionally, it can identify disordered regions within proteins with an accuracy comparable to the most sophisticated existing disorder predictors. Remarkably, DynaMine achieves this high performance without depending on prior disorder knowledge or three-dimensional structural information, which makes it a unique approach on the field as well as providing independent proof of the relationship between dynamics and structural disorder in protein regions.
Finally, the predicted values have a clear physical meaning: they are relevant on an absolute scale and go beyond the binary classification of the predicted residues as ordered or disordered, so allowing for direct dynamics comparisons between protein regions.