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Related Experiment Videos

BOLD--a biological O-linked glycan database.

C A Cooper1, M R Wilkins, K L Williams

  • 1Department of Chemistry, Macquarie University, North Ryde, Australia. catherine.cooper@proteomesystems.com

Electrophoresis
|December 28, 1999
PubMed
Summary
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O-linked glycans, complex carbohydrate structures attached to proteins, exhibit diverse compositions and linkages. The Biological O-linked Database (BOLD) consolidates information on these structures, aiding glycobiology research.

Area of Science:

  • Glycobiology
  • Proteomics
  • Bioinformatics

Background:

  • O-linked glycans are protein modifications involving diverse monosaccharides attached via hydroxyl groups.
  • These structures can range from simple monosaccharides to complex oligosaccharides with various additions.
  • O-linked glycans can also incorporate sulfate and phosphate residues, increasing structural diversity.

Purpose of the Study:

  • To describe the Biological O-linked Database (BOLD).
  • To provide a centralized resource for O-linked glycan structures.
  • To facilitate research in glycobiology by cataloging known O-linked glycans.

Main Methods:

  • Development of a relational database (BOLD).
  • Integration of data on glycan structures, biological sources, and references.

Related Experiment Videos

  • Linking to external databases like SWISS-PROT and MEDLINE for comprehensive information.

    • Main Results:

    • BOLD contains information on numerous O-linked glycan structures.
    • The database links glycan structures to their protein sources across species and tissues.
    • References and methods for glycan structure determination are included.

    Conclusions:

    • BOLD serves as a valuable resource for glycobiology researchers.
    • The database aids in understanding the diversity and biological relevance of O-linked glycans.
    • Facilitates comparative analysis of O-linked glycosylation across different biological contexts.