Because AWSEM's potential is analytical and differentiable, it is currently implemented as a molecular dynamics algorithm (AWSEM-MD).

In the latter case it relies solely on sequence information. AWSEM naturally covers the whole spectrum between native-structure-based and de novo methods, and can be used both with the knowledge of native structures, and without such explicit knowledge. The AWSEM potential is a prominent member of this latter group, where various research groups have successfully demonstrated its broad applications in monomeric protein structure prediction, binding predictions of dimers and multimeric assemblies, folding of membrane proteins, and structural and kinetic studies of protein-DNA complexes. To address such problems, several coarse-grained protein force fields have been developed in the last 30 years or so that allow de novo structure prediction even in the absence of sequence homology. These methods, however, cannot be used when the target protein structure is unknown or non-native interactions play a significant role. In particular, many useful coarse-grained protein force fields require prior knowledge of the native structure for the specific protein target, often with the stated goal of simulating protein folding kinetics and dynamics. The latter approaches, which enable treating large systems at long timescales, come in with rather broad variety of choices, compared with the atomistic models. Proteins and other biomolecules can be simulated on a computer primarily in two ways: relying either on atomistic or coarse-grained force fields.

Force 20 fortran download