title: Folding and self-assembly of a small heterotetramer.
abstract: Designed miniproteins offer a possibility to study folding and association of protein complexes, both experimentally and in silico. Using replica exchange molecular dynamics and the coarse-grain UNRES force field, we have simulated the folding and self-assembly of the heterotetramer BBAThet1, comparing it with that of the homotetramer BBAT1 which has the same size and ββα-fold. For both proteins, association of the tetramer precedes and facilitates folding of the individual chains.
authors.affiliation: Department of Physics Engineering, Hacettepe University, Beytepe-Ankara 06800, Turkey.
authors.forename: Fatih
authors.initials: F
authors.lastname: Yaşar
authors.affiliation: Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-952 Gdańsk, Poland.
authors.forename: Adam K
authors.initials: AK
authors.lastname: Sieradzan
authors.affiliation: Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019-5251, USA.
authors.forename: Ulrich H E
authors.initials: UH
authors.lastname: Hansmann
mesh_terms: D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
chemical_list: D011506:Proteins