Ramalli, S.G. and Miles, Andrew and Janes, R.W. and Wallace, Bonnie A. (2022) The PCDDB (Protein Circular Dichroism Data Bank): a bioinformatics resource for protein characterisations and methods development. Journal of Molecular Biology 434 (11), p. 167441. ISSN 0022-2836.
|
Text
47259.pdf - Author's Accepted Manuscript Available under License Creative Commons Attribution Non-commercial No Derivatives. Download (1MB) | Preview |
Abstract
The Protein Circular Dichroism Data Bank (PCDDB) [https://pcddb.cryst.bbk.ac.uk] is an established resource for the biological, biophysical, chemical, bioinformatics, and molecular biology communities. It is a freely-accessible repository of validated protein circular dichroism (CD) spectra and associated sample and other metadata, with entries having links to other bioinformatics resources including, amongst others, structure (PDB) and sequence (UniProt) databases, as well as to published papers which produced the data and cite the database entries. It includes primary (unprocessed) and final (processed) spectral data, which are available in both text and pictorial formats, as well as detailed sample and validation information produced for each of the entries. Recently the metadata content associated with each of the entries, as well as the number and structural breadth of the protein components included, have been expanded. The PCDDB includes data on both wild-type and mutant proteins, and because CD studies primarily examine proteins in solution, it also contains examples of the effects of different environments on their structures, plus thermal unfolding/folding series. Methods for both sequence and spectral comparisons are included. The data included in the PCDDB complement results from crystal, cryo-electron microscopy, NMR spectroscopy, bioinformatics characterisations and classifications, and other structural information available for the proteins via links to other databases. The entries in the PCDDB have been used for the development of new analytical methodologies, for interpreting spectral and other biophysical data, and for providing insight into structures and functions of individual soluble and membrane proteins and protein complexes.
Metadata
Item Type: | Article |
---|---|
Keyword(s) / Subject(s): | Circular dichroism spectroscopy, protein structural and spectroscopic database, data deposition and accession, protein stability and environmental effects, resource for bioinformatic developments |
School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
Depositing User: | Administrator |
Date Deposited: | 13 Jan 2022 14:16 |
Last Modified: | 02 Aug 2023 18:15 |
URI: | https://eprints.bbk.ac.uk/id/eprint/47259 |
Statistics
Additional statistics are available via IRStats2.