Journal article
Assembly of Stefin B into Polymorphic Oligomers Probed by Discrete Molecular Dynamics
Journal of chemical theory and computation, v 11(5), pp 2355-2366
12 May 2015
PMID: 26574430
Featured in Collection : UN Sustainable Development Goals @ Drexel
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.
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Details
- Title
- Assembly of Stefin B into Polymorphic Oligomers Probed by Discrete Molecular Dynamics
- Creators
- Matjaž Žganec - Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute , 1000 Ljubljana, SloveniaEva Žerovnik - Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute , 1000 Ljubljana, SloveniaBrigita Urbanc - Department of Physics, Drexel University , Philadelphia, Pennsylvania 19104, United States
- Publication Details
- Journal of chemical theory and computation, v 11(5), pp 2355-2366
- Publisher
- American Chemical Society; Washington, DC
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000354578900035
- Scopus ID
- 2-s2.0-84929167465
- Other Identifier
- 991014877774004721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Chemistry, Physical
- Physics, Atomic, Molecular & Chemical