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Related Concept Videos

Protein Families02:47

Protein Families

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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Protein Organization01:24

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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The Protein Ensemble Database.

Mihaly Varadi1,2, Peter Tompa3,4,5

  • 1Department of Structural Biology, Vlaams Institute voor Biotechnologie (VIB), Brussels, Belgium.

Advances in Experimental Medicine and Biology
|September 21, 2015
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) lack stable structures, making them crucial in modern structural biology. The new Protein Ensemble Database (PEDb) offers vital data for understanding IDP function and flexibility.

Keywords:
Calculation protocolsDatabaseEnsembles of structuresExperimental validation

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Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • The classical structure-function paradigm is challenged by intrinsically disordered proteins (IDPs).
  • IDPs exhibit inherent structural heterogeneity crucial for their function.
  • Characterizing IDPs requires specialized biophysical techniques due to their flexibility.

Purpose of the Study:

  • To introduce the Protein Ensemble Database (PEDb) as a novel resource for IDP research.
  • To provide a centralized, accessible repository for IDP structural ensemble data.
  • To facilitate advancements in computational modeling and understanding of IDP function.

Main Methods:

  • Utilized experimental data from small-angle X-ray scattering (SAXS) and nuclear magnetic resonance (NMR) spectroscopy.
  • Employed computational methods to derive structural ensembles representing protein conformational sampling.
  • Manually curated data and associated calculation protocols for the database.

Main Results:

  • Established the Protein Ensemble Database (PEDb) as the first open-access resource for IDP ensemble models.
  • Integrated primary experimental data (SAXS/NMR) with computational models.
  • Ensured manual curation for data quality and accessibility.

Conclusions:

  • The Protein Ensemble Database (PEDb) will accelerate research on intrinsically disordered proteins.
  • Free access to curated data promotes the development of advanced modeling techniques.
  • PEDb facilitates a deeper understanding of how protein disorder relates to biological function.