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Related Concept Videos

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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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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Updated: Oct 18, 2025

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Phase separation vs aggregation behavior for model disordered proteins.

Ushnish Rana1, Clifford P Brangwynne1, Athanassios Z Panagiotopoulos1

  • 1Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, USA.

The Journal of Chemical Physics
|October 2, 2021
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Summary
This summary is machine-generated.

Sequence properties control protein phase separation. A normalized sequence charge decoration (SCD) parameter predicts whether proteins form large phases or small aggregates, linking sequence to cellular organization.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Cell Biology

Background:

  • Liquid-liquid phase separation (LLPS) is crucial for cellular organization and biochemical regulation.
  • Protein LLPS is sequence-dependent, but sequence features dictating phase transition and morphology remain unclear.

Purpose of the Study:

  • To investigate how sequence distribution, sticker fraction, and chain length influence protein phase separation versus finite aggregation.
  • To identify sequence properties that predict the type of phase transition in disordered proteins.

Main Methods:

  • Employed grand canonical Monte Carlo simulations.
  • Utilized a coarse-grained model for disordered proteins.
  • Systematically varied sequence distribution, sticker fraction, and chain length.

Main Results:

  • Introduced a normalized sequence charge decoration (SCD) parameter as a predictive criterion for macroscopic phase separation versus finite aggregation.
  • Demonstrated a strong correlation between the SCD parameter and the critical density for phase separation.
  • Found that longer chain lengths generally favor macroscopic phase separation for most sequences.

Conclusions:

  • The SCD parameter provides a quantitative link between protein sequence properties and phase behavior.
  • Macroscopic LLPS is likely the dominant phase transition for disordered proteins with dominant short-ranged attractive interactions.
  • Findings offer insights into the widespread observation of LLPS in cellular environments.