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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.

SUBMITTER: Berhanu WM

PROVIDER: S-EPMC4201375 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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

Berhanu W M WM Jiang P P Hansmann U H E UH

Physical review. E, Statistical, nonlinear, and soft matter physics 20130111 1

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. ...[more]

PMID: 23410475

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