title: Assembly of Stefin B into Polymorphic Oligomers Probed by Discrete Molecular Dynamics.
abstract: Assembly of an amyloidogenic protein stefin B into molten globule oligomers is studied by efficient discrete molecular dynamics. Consistent with in vitro findings, tetramers form primarily through dimer association, resulting in a decreased trimer abundance. Oligomers up to heptamers display elongated rod-like morphologies akin to protofibrils, whereas larger oligomers, decamers through dodecamers, form elongated, branched, as well as annular structures, providing structural insights into pore forming ability and toxicity of amyloidogenic proteins.
authors.affiliation: Faculty of Mathematics and Physics, University of Ljubljana , 1000 Ljubljana, Slovenia.|Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute , 1000 Ljubljana, Slovenia.
authors.forename: Matjaž
authors.initials: M
authors.lastname: Žganec
authors.affiliation: Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute , 1000 Ljubljana, Slovenia.
authors.forename: Eva
authors.initials: E
authors.lastname: Žerovnik
authors.affiliation: Faculty of Mathematics and Physics, University of Ljubljana , 1000 Ljubljana, Slovenia.|Department of Physics, Drexel University , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Brigita
authors.initials: B
authors.lastname: Urbanc
mesh_terms: D055313:Cystatin B / Q000737:chemistry* / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D055313:Cystatin B