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Emergence of order in self-assembly of the intrinsically disordered biomineralisation peptide n16N

Rutter, G. O., Brown, A. H., Quigley, D., Walsh, T. R. and Allen, M. P. 2018, Emergence of order in self-assembly of the intrinsically disordered biomineralisation peptide n16N, Molecular simulation, vol. 44, no. 6, pp. 463-469, doi: 10.1080/08927022.2017.1405158.

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Title Emergence of order in self-assembly of the intrinsically disordered biomineralisation peptide n16N
Author(s) Rutter, G. O.
Brown, A. H.
Quigley, D.
Walsh, T. R.ORCID iD for Walsh, T. R. orcid.org/0000-0002-0233-9484
Allen, M. P.
Journal name Molecular simulation
Volume number 44
Issue number 6
Start page 463
End page 469
Total pages 7
Publisher Taylor & Francis
Place of publication Abingdon, Eng.
Publication date 2018-04
ISSN 0892-7022
1029-0435
Keyword(s) Science & Technology
Physical Sciences
Chemistry, Physical
Physics, Atomic, Molecular & Chemical
Chemistry
Physics
Proteins
coarse-grained
aggregation
biomineralisation
MOLECULAR-DYNAMICS
CRYSTAL-GROWTH
PINCTADA-FUCATA
MATRIX PROTEIN
ORGANIC MATRIX
NACRE PROTEIN
OYSTER SHELL
MONTE-CARLO
IN-VITRO
SIMULATION
Summary 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.
Language eng
DOI 10.1080/08927022.2017.1405158
Field of Research 02 Physical Sciences
03 Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2017, The Authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30111156

Document type: Journal Article
Collections: Institute for Frontier Materials
Open Access Collection
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