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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

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Updated: Jun 7, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

No Time to Fold: Intrinsically Disordered Microproteins in Action.

Tianyu Chen1, Kevin Cao1, Thomas F Martinez1,2,3

  • 1Department of Pharmaceutical Sciences, University of California, Irvine, Irvine, California 92617, United States.

Biochemistry
|June 5, 2026
PubMed
Summary
This summary is machine-generated.

Discovered microproteins, small protein regulators, are often intrinsically disordered. Studying these disordered microproteins enhances understanding of cellular processes and disease therapeutics.

Keywords:
intrinsically disordered proteinmicroproteinsmall open reading frame

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Last Updated: Jun 7, 2026

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Published on: April 5, 2013

Area of Science:

  • Molecular Biology
  • Genomics
  • Proteomics

Background:

  • Genomics and proteomics reveal thousands of microproteins encoded by small open reading frames.
  • Microproteins are often intrinsically disordered, rich in disorder-promoting amino acids.
  • These small proteins regulate key cellular functions like DNA repair and metabolism.

Purpose of the Study:

  • To review the functions and mechanisms of disordered microproteins.
  • To explore methods for studying their disordered nature.
  • To discuss post-translational modifications and therapeutic targeting of microproteins.

Main Methods:

  • Bioinformatic analysis of genomic and proteomic data.
  • Prediction of intrinsic disorder based on amino acid composition.
  • Literature review of characterized microproteins and their functions.
  • Analysis of post-translational modifications and therapeutic strategies.

Main Results:

  • Microproteins regulate diverse cellular processes, acting similarly to intrinsically disordered proteins (IDPs).
  • Many microproteins are intrinsically disordered, influencing protein complex regulation.
  • Post-translational modifications impact microprotein function and regulation.

Conclusions:

  • Disordered microproteins are crucial regulators of cellular processes.
  • Collaborative research between microprotein and IDP fields is vital.
  • Targeting disordered microproteins offers potential therapeutic strategies for diseases.