title: Geometrical constraints limiting the poly(ADP-ribose) conformation investigated by molecular dynamics simulation.
abstract: Poly(ADP-ribosylation) is a post-transductional modification that regulates protein's function. Most of the proteins subjected to this control mechanism belong to machineries involved in DNA damage repair, or DNA interacting proteins. Poly(ADP-ribose) polymers are long chains of even 100 monomer length that can be branched at several positions but, not withstanding its importance, nothing is known concerning its structure. To understand, which are the geometrical parameters that confer to the polymer the structural constraints that determine its interaction with the target proteins, we have performed molecular dynamics of three chains of different length, made by 5, 25, and 30 units, the last one being branched. Analysis of the simulations allowed us to identify the main intra- and inter-monomer dihedral angles that govern the structure of the polymer that however, does not reach a unique definite conformation.
authors.affiliation: Department of Biology and Centro di Bioinformatica e Biostatistica, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome, 00133, Italy.
authors.forename: Ilda
authors.initials: I
authors.lastname: D'Annessa
authors.forename: Andrea
authors.initials: A
authors.lastname: Coletta
authors.forename: Alessandro
authors.initials: A
authors.lastname: Desideri
mesh_terms: D004249:DNA Damage; D004260:DNA Repair; D008968:Molecular Conformation; D056004:Molecular Dynamics Simulation; D011064:Poly Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases
chemical_list: D011064:Poly Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases
keywords: dihedral angles; molecular dynamics; poly(ADP-ribose); polymer