Assessing SIRAH’s Capability to Simulate Intrinsically Disordered Proteins and Peptides
Florencia Klein, Exequiel Barrera, Sergio Pantano
Abstract
The challenges posed by intrinsically disordered proteins (IDPs) to atomistic and coarse-grained (CG) simulations are boosting efforts to develop and reparametrize current force fields. An assessment of the dynamical behavior of IDPs' and unstructured peptides with the CG SIRAH force field suggests that the current version achieves a fair description of IDPs' conformational flexibility. Moreover, we found a remarkable capability to capture the effect of point mutations in loosely structured peptides.
Topics & Concepts
Intrinsically disordered proteinsBoosting (machine learning)Flexibility (engineering)Computer scienceMolecular dynamicsNanotechnologyForce field (fiction)Current (fluid)Computational biologyPhysicsBiophysicsChemistryMaterials scienceArtificial intelligenceBiologyComputational chemistryMathematicsStatisticsThermodynamicsProtein Structure and DynamicsEnzyme Structure and FunctionBacteriophages and microbial interactions