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Conservation of Protein Domains02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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CD Spectroscopy to Study DNA-Protein Interactions
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PCDDB: new developments at the Protein Circular Dichroism Data Bank.

Lee Whitmore1, Andrew John Miles1, Lazaros Mavridis2

  • 1Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, UK.

Nucleic Acids Research
|September 11, 2016
PubMed
Summary
This summary is machine-generated.

The Protein Circular Dichroism Data Bank (PCDDB) is a public repository for circular dichroism data. It has been enhanced with improved data display, search algorithms, and increased holdings, serving structural biology and related fields.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Bioinformatics

Background:

  • The Protein Circular Dichroism Data Bank (PCDDB) serves as a public repository for circular dichroism (CD) spectroscopic data.
  • It archives experimental data alongside crucial bioinformatics and experimental metadata.

Purpose of the Study:

  • To detail the ongoing developments and improvements within the PCDDB over its 5+ years of operation.
  • To highlight the repository's role in data sharing and its impact on scientific research.

Main Methods:

  • Continuous updates to data display, searching algorithms, and data formats.
  • Inclusion of detailed experimental methods, calculations, and links to bioinformatics databases.
  • Validation techniques and expansion of data holdings.

Main Results:

  • Significant enhancements in data accessibility, search functionality, and content.
  • Increased number of archived datasets and associated metadata.
  • Broad adoption and usage by structural biology, bioinformatics, analytical, and pharmaceutical communities.

Conclusions:

  • The PCDDB has evolved into a vital resource for researchers in structural biology and related fields.
  • The repository facilitates new software and methods development through freely accessible data.
  • Ongoing improvements ensure the PCDDB remains a valuable public data archive.