title: Conformational analysis of aqueous BMP-2 using atomistic molecular dynamics simulations.
abstract: BMP-2 is an osteoinductive protein, involved in the differentiation and proliferation of osteoblasts, with potential application as bioactive agent in bone implants and scaffolds. Since the three-dimensional structure of a protein usually determines its bioactivity, in order to efficiently design bone implants activated with BMP-2 it is essential to identify the factors influencing the protein conformation. In the present work, atomistic molecular dynamics simulations are employed to investigate the BMP-2 monomer and homodimer in vacuum and water. The influence of each environment on the BMP-2 structure is analyzed regarding protein structural changes and energy contributions driving the BMP-2 conformation.
authors.affiliation: Physikalische Chemie, Technische Universität Dresden, Dresden, Germany. augusto.oliveira@chemie.tu-dresden.de
authors.forename: Augusto F
authors.initials: AF
authors.lastname: Oliveira
authors.forename: Sibylle
authors.initials: S
authors.lastname: Gemming
authors.forename: Gotthard
authors.initials: G
authors.lastname: Seifert
mesh_terms: D055396:Bone Morphogenetic Protein 2 / Q000737:chemistry*; D019281:Dimerization; D056004:Molecular Dynamics Simulation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013816:Thermodynamics; D014618:Vacuum; D014867:Water / Q000737:chemistry
chemical_list: D055396:Bone Morphogenetic Protein 2; D014867:Water