From protein sequence to dynamics and disorder with DynaMine

Protein function and dynamics are closely related, but accurate dynamics information is difficult to obtain. Based on a carefully assembled dataset derived from experimental data for proteins in solution, we develop DynaMine, a fast, high-quality predictor of protein backbone dynamics. DynaMine uses only protein sequence information as input and shows great potential in distinguishing regions of different structural organization, such as folded domains, disordered linkers, molten globules and pre-structured binding motifs of different sizes. It also identifies disordered regions within proteins with an accuracy comparable to the most sophisticated existing predictors, without depending on prior disorder knowledge or structural information. DynaMine provides molecular biologists with an important new method that grasps the dynamical characteristics of any protein of interest, as demonstrated here for human p53.