walsh-emergenceoforder-2018.pdf (1.26 MB)
Emergence of order in self-assembly of the intrinsically disordered biomineralisation peptide n16N
journal contribution
posted on 2018-04-01, 00:00 authored by G O Rutter, A H Brown, D Quigley, Tiffany WalshTiffany Walsh, M P Allen© 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. We present the results of an aggregation study on the intrinsically disordered biomineralisation peptide n16N, which selects the aragonite polymorph of calcium carbonate and is expected to have aggregation-dependent structure and function. The peptide is a sub-sequence of the in vivo protein n16, with putative framework and polymorph selection roles in the nacre layer of pearl oyster (Pinctada fucata). Employing the intermediate-resolution coarse-grained protein model PLUM*, which has previously been validated with respect to n16N, we simulate assemblies of these peptide units for system sizes inaccessible to atomistic models. We use extensive conformational sampling to show that the configurational ensemble explored by n16N aggregates contains a significant proportion of ordered β-structure, within which arrangement of monomers is consistent with a previous hypothesis on functionally distinct subdomains of n16N. We also study an n16N mutant which fails to aggregate in experimental studies and obtain very similar behaviour, the consequences of which are discussed.
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Journal
Molecular simulationVolume
44Issue
6Pagination
463 - 469Publisher
Taylor & FrancisLocation
Abingdon, Eng.Publisher DOI
Link to full text
ISSN
0892-7022eISSN
1029-0435Language
engPublication classification
C1 Refereed article in a scholarly journalCopyright notice
2017, The AuthorsUsage metrics
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