The Library
Data for Emergence of order in self-assembly of the intrinsically disordered biomineralisation peptide n16N
Tools
Tools
Tools
Rutter, Gil (2017) Data for Emergence of order in self-assembly of the intrinsically disordered biomineralisation peptide n16N. [Dataset]
![[img]](http://wrap.warwick.ac.uk/style/images/fileicons/application_zip.png) |
Archive (ZIP) (Dataset and README files)
data.zip - Published Version Available under License Creative Commons Attribution 4.0. Download (940Kb) |
Abstract
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 beta-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.
| Item Type: | Dataset | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry | ||||||||||||||||||
| Divisions: | Faculty of Science > Physics | ||||||||||||||||||
| Type of Data: | Molecular structure and structure analysis data | ||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Self-assembly (Chemistry), Biomineralization, Peptides | ||||||||||||||||||
| Publisher: | Physics, University of Warwick | ||||||||||||||||||
| Official Date: | 19 July 2017 | ||||||||||||||||||
| Dates: |
|
||||||||||||||||||
| Collection date: |
|
||||||||||||||||||
| Status: | Not Peer Reviewed | ||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||
| Media of Output: | .pickle, .ARG, .NUMPY, .PDB and .VMD files | ||||||||||||||||||
| Access rights to Published version: | Open Access | ||||||||||||||||||
| Copyright Holders: | University of Warwick | ||||||||||||||||||
| Description: | The dataset is composed of .pickle files (PYTHON), .agr files (open with xmgrace. This is a standard (free and open source) Unix/Linux plotting tool https://en.wikipedia.org/wiki/Grace_(plotting_tool)), .numpy files (a standard format for reading arrays into numerical Python using the numpy.fromfile function) and .pdb files (Protein DataBank files, a standard open format for representing molecular structures. They can be opened in a number of programs. One of these is VMD (Visual Molecular Dynamics) and the .vmd files are input scripts for that software which will read and render the molecular structures. https://en.wikipedia.org/wiki/Visual_Molecular_Dynamics ) |
||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
||||||||||||||||||
| Related URLs: | |||||||||||||||||||
| Contributors: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
