title: Folding and association of a homotetrameric protein complex in an all-atom Go model.
abstract: The 84-residue homotetrameric BBAT1 is one of the smallest stable protein complexes and therefore is a good test system to study the self-assembly of multimeric proteins. We have researched for this protein the interplay between the folding of monomers and their assembly into tetramers. Replica exchange molecular dynamics simulations relying on a Go model are compared with earlier simulations that use the physics-based coarse-grained UNRES model.
authors: Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019-5251, USA.
authors: W M
authors: WM
authors: Berhanu
authors: P
authors: P
authors: Jiang
authors: U H E
authors: UH
authors: Hansmann
mesh_terms: D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D011506:Proteins