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Related Concept Videos

Condensins02:15

Condensins

Condensins are large protein complexes that use ATP to fuel the assembly of chromosomes during mitosis. They transform the tangled, shapeless mass of post-interphase DNA into individualized chromosomes by compacting, organizing, and segregating chromosomal DNA.
The plant and animal cells contain two types of condensin complexes—condensin I and condensin II. Both complexes have five subunits: two SMC (Structural Maintenance of Chromosomes) subunits, a kleisin subunit, and two HEAT-repeat...
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Phase Transitions: Vaporization and Condensation

The physical form of a substance changes on changing its temperature. For example, raising the temperature of a liquid causes the liquid to vaporize (convert into vapor). The process is called vaporization—a surface phenomenon. Vaporization occurs when the thermal motion of the molecules overcome the intermolecular forces, and the molecules (at the surface) escape into the gaseous state. When a liquid vaporizes in a closed container, gas molecules cannot escape. As these gas phase molecules...
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Protein Folding

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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
Dehydration Synthesis01:15

Dehydration Synthesis

Dehydration synthesis (also called a condensation reaction) is the chemical process in which two molecules covalently link together to form a new molecule, along with the release of a water molecule. Many physiologically important compounds form by dehydration synthesis reactions, such as complex carbohydrates, proteins, DNA, and RNA.Synthesis of carbohydratesSugar molecules are covalently linked together by dehydration synthesis. During the reaction, the hydroxyl (-OH) group from one reactant...

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Related Experiment Video

Updated: Jul 15, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

A Glimpse into the Initial Microsecond of Biomolecular Condensation.

Longchen Zhu1, Guohong Liao2,3, Yumeng Zhang4

  • 1Department of Chemistry, Westlake University, 600 Dunyu Road, Hangzhou 310030 Zhejiang, P. R. China.

Journal of the American Chemical Society
|July 14, 2026
PubMed
Summary

Cellular biomolecular condensation, crucial for physiological activities, was studied in its initial moments. Backbone hydrogen bonding, not hydrophobicity, was found to be key for ultrafast peptide condensation and assembly.

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Last Updated: Jul 15, 2026

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Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions
09:01

Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions

Published on: April 17, 2026

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Biomolecular condensation is essential for cellular function.
  • The initial stages of phase transition during condensation are not well understood.

Purpose of the Study:

  • To investigate the molecular events and kinetics during the first microsecond of peptide condensation.
  • To elucidate the role of different molecular forces in the early stages of biomolecular phase transitions.

Main Methods:

  • Temperature jump infrared spectroscopy was employed to probe rapid structural changes.
  • Molecular dynamics simulations provided high-resolution insights into the condensation process.

Main Results:

  • Intrinsically disordered proteins undergo structural transitions and assembly on ultrafast timescales.
  • Backbone hydrogen bonding, rather than hydrophobicity, was identified as the primary mediator for stabilizing local structures during initial condensation.
  • Hydrogen bonds facilitate the formation of stable interaction interfaces, enabling preorganized conformations.

Conclusions:

  • Hydrogen bonding plays a critical role in the ultrafast condensation of hydrophobic polypeptides.
  • This mechanism allows disordered proteins to adopt specific conformations and influences assembly kinetics in cellular environments.