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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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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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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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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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An Integrated Approach for Microprotein Identification and Sequence Analysis
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Small proteins can no longer be ignored.

Gisela Storz1, Yuri I Wolf, Kumaran S Ramamurthi

  • 1Cell Biology and Metabolism Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-5430;

Annual Review of Biochemistry
|March 11, 2014
PubMed
Summary

Small proteins, defined as 50 amino acids or fewer, are increasingly discovered and play diverse roles, especially at bacterial membranes. Future research will uncover more functions of these overlooked proteins.

Keywords:
cell divisionmembraneproteinsignal transductionsporulationtransport

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genomics

Background:

  • Small proteins (≤50 amino acids) have been historically overlooked due to annotation and detection challenges.
  • Recent advances reveal numerous small proteins encoded by intergenic regions and small regulatory RNAs.
  • Comparative sequence analysis suggests widespread synthesis of small proteins in organisms.

Purpose of the Study:

  • To review the known functions of bacterial small proteins.
  • To highlight the diverse biological processes regulated by small proteins.
  • To identify key questions for future research on these molecules.

Main Methods:

  • Literature review of identified small proteins and their functions.
  • Analysis of recent discoveries from genetic and RNA studies.
  • Comparative sequence analysis.

Main Results:

  • A significant number of small proteins are synthesized in organisms.
  • Many bacterial small proteins function at the cellular membrane.
  • These proteins are involved in a wide array of biological processes.

Conclusions:

  • Small proteins are functionally important and widely distributed.
  • Their roles, particularly at membranes, are diverse and critical.
  • Further investigation is needed to fully understand their biological significance.