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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Proteomics01:33

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Conservation of Protein Domains Over Different Proteins02:26

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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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Protein-protein Interfaces02:04

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Aggregation prone regions in human proteome: Insights from large-scale data analyses.

R Prabakaran1, Dhruv Goel2, Sandeep Kumar3

  • 1Department of Biotechnology, Bhupat Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.

Proteins
|March 4, 2017
PubMed
Summary

The human proteome contains numerous aggregation-prone regions (APRs) that are actively managed through sequence optimization. These APRs play diverse roles in protein structure and function, offering insights for drug discovery.

Keywords:
aggregationdiseaseshuman proteomepredictionprotein functionprotein stability

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Area of Science:

  • Biochemistry
  • Proteomics
  • Structural Biology

Background:

  • Protein aggregation causes human diseases, yet the proteome's defense mechanisms are poorly understood.
  • Aggregation-prone regions (APRs) are implicated in amyloid formation and disease pathology.

Purpose of the Study:

  • To survey the human proteome for the incidence and characteristics of APRs.
  • To understand how the human proteome manages APRs and their functional implications.

Main Methods:

  • Analysis of experimentally validated amyloid-fibril forming peptides.
  • Computational prediction of potential APRs across the human proteome.
  • Sequence randomization to assess the significance of observed APR incidence.

Main Results:

  • 260 human proteins (1% of proteome) contain experimentally validated amyloid-fibril segments.
  • Computational predictions indicate over 80% of human proteins have potential APRs.
  • APRs are strategically located near active/ligand sites and heterotypic interfaces, not PTM sites.
  • Human protein sequences show significant reduction in APR incidence via specific amino acid composition and patterning.

Conclusions:

  • The human proteome actively manages APRs using sequence-structural strategies, balancing risks and benefits.
  • APRs have multifaceted roles in protein sequence-structure-function relationships.
  • Understanding APRs offers potential for novel drug discovery and development.