Folding and association of a homotetrameric protein complex in an all-atom Go model

W. M. Berhanu, P. Jiang, and U. H. E. Hansmann
Phys. Rev. E 87, 014701 – Published 11 January 2013

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.

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  • Received 14 September 2012

DOI:https://doi.org/10.1103/PhysRevE.87.014701

©2013 American Physical Society

Authors & Affiliations

W. M. Berhanu, P. Jiang, and U. H. E. Hansmann

  • Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019-5251, USA

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Vol. 87, Iss. 1 — January 2013

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