Intrinsically disordered proteins are biomolecules that do not have a definite 3D structure; therefore, their dynamical simulation cannot start from a known list of atomistic positions, such as a Protein Data Bank file. We describe a method to start a computer simulation of these proteins. The first step of the procedure is the creation of a multi-rod configuration of the molecule, derived from its primary sequence. This structure is dynamically evolved in vacuo until its gyration radius reaches the experimental average value; at this point solvent molecules, in explicit or implicit implementation, are added to the protein and a regular molecular dynamics simulation follows. We have applied this procedure to the simulation of tau, one of the largest totally disordered proteins.
|Titolo:||Molecular dynamics simulation of intrinsically disordered proteins|
|Autori:||Battisti, A.; Tenenbaum, A.|
|Data di pubblicazione:||2012|
|Digital Object Identifier (DOI):||10.1080/08927022.2011.608671|
|Appare nelle tipologie:||1.1 Journal article|