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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Mechanical Protein Function01:58

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 

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Related Experiment Video

Updated: May 20, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

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Published on: January 26, 2016

Moonlighting peptides with emerging function.

Jonathan G Rodríguez Plaza1, Amanda Villalón Rojas, Sur Herrera

  • 1Biochemistry and Structural Biology Department, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México DF, México.

Plos One
|July 19, 2012
PubMed
Summary
This summary is machine-generated.

Scientists engineered novel moonlighting peptides, combining multiple functions within a single protein. These peptides demonstrated a new cell-death-inducing function in yeast, highlighting emergent properties in protein evolution.

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Last Updated: May 20, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

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Published on: January 26, 2016

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Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Proteins can exhibit multiple functions, often through distinct domains.
  • The evolution of multi-functional proteins, or moonlighting proteins, is not fully understood.
  • Emergent functions from combined activities within a single domain are hypothesized but underexplored.

Purpose of the Study:

  • To investigate if combining two activities in a single protein domain can lead to emergent functions.
  • To design and test novel moonlighting peptides using proposed evolutionary mechanisms.
  • To demonstrate a new function arising from engineered multi-activity peptides.

Main Methods:

  • Designing peptides incorporating two distinct functional activities.
  • Utilizing mutation of non-functional residues as an evolutionary strategy.
  • Employing natively unfolded peptides in the design process.
  • Assessing peptide function and emergent properties in yeast models.

Main Results:

  • Engineered moonlighting peptides successfully combined two independent activities.
  • The combined activities resulted in a novel emergent function: inducing cell death in yeast.
  • Demonstrated the feasibility of creating moonlighting proteins through specific design strategies.

Conclusions:

  • Combining multiple protein activities within a single domain can generate emergent functions.
  • This provides a potential evolutionary mechanism for the development of moonlighting proteins.
  • Moonlighting proteins contribute to biological complexity through unappreciated emergent properties.