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Related Concept Videos

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

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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at 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...
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...

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Related Experiment Video

Updated: May 14, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

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Published on: April 26, 2013

Programmable DNA Folding Modulates Phase Behavior and Dynamics of DNA/Peptide Condensates.

Itai Katzir1, Yanbing Wen2, Inbal Razi1

  • 1Shmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.

ACS Nano
|May 13, 2026
PubMed
Summary
This summary is machine-generated.

Nucleic acid folding influences liquid-liquid phase separation (LLPS). An HIV peptide modulates this process, with DNA order suppressing LLPS and disorder enhancing it, impacting viral genome organization.

Keywords:
Biomolecular condensatesCoacervatesDNALiquid−liquid phase separation (LLPS)Peptide

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Virology

Background:

  • Membraneless compartments formed by liquid-liquid phase separation (LLPS) are crucial for biological processes, including viral replication.
  • Nucleocapsid (NC) protein in retroviruses guides RNA folding and assembly for efficient viral particle packaging.

Purpose of the Study:

  • To investigate how nucleic acid folding and structure affect LLPS.
  • To determine if an HIV NC-derived peptide (HNP) can modulate LLPS through chaperone activity.

Main Methods:

  • Designed a programmable single-stranded DNA (ssDNA) library with varying folding and palindromic architectures.
  • Employed circular dichroism, FRET, SAXS, and coarse-grained simulations to analyze DNA conformations and phase behavior.
  • Correlated DNA structural order and dimerization with condensate properties like viscosity.

Main Results:

  • HNP interactions promote DNA folding.
  • Increased DNA order suppresses LLPS, while structural disorder enhances it.
  • Palindromic linkers inducing DNA dimerization increase phase separation and condensate viscosity.

Conclusions:

  • Identified local structural order and palindromic dimerization as key programmable determinants of DNA/peptide condensate behavior.
  • Provided mechanistic insights into viral genome organization.
  • Offered principles for tuning the properties of synthetic condensates.