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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
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Updated: May 21, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Characterizing intermolecular interactions that initiate native-like protein aggregation.

Francesco Bemporad1, Alfonso De Simone, Fabrizio Chiti

  • 1Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.

Biophysical Journal
|June 21, 2012
PubMed
Summary
This summary is machine-generated.

Folded proteins can aggregate without unfolding. This study reveals a novel self-assembly mechanism in acylphosphatase (Sso AcP) involving increased flexibility and intermolecular interactions in a native-like state (N*).

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Last Updated: May 21, 2026

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12:58

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Published on: September 12, 2019

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Area of Science:

  • Biochemistry
  • Protein Dynamics
  • Molecular Biophysics

Background:

  • Protein aggregation is a hallmark of many diseases and can occur from various conformational states.
  • Understanding the initial steps of protein aggregation is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To characterize the early aggregation events of acylphosphatase from Sulfolobus solfataricus (Sso AcP).
  • To elucidate the role of native-like states in protein self-assembly.

Main Methods:

  • Computer simulations integrated with experimental hydrogen/deuterium (H/D) exchange data.
  • Direct measurements using H/D exchange rates, isothermal titration calorimetry, and intermolecular relaxation enhancements.

Main Results:

  • Sso AcP populates a native-like state (N*) with increased dynamics and hydrodynamic radius under aggregation-promoting conditions, without local unfolding.
  • A specific edge strand gains affinity for an unfolded segment within the N* state.
  • Antiparallel intermolecular interactions form between the edge strand and the unfolded segment in the N* state, but not in the fully native state.

Conclusions:

  • A novel self-assembly mechanism for folded proteins is identified, driven by increased flexibility of aggregation-prone segments.
  • This mechanism bypasses the need for complete unfolding to initiate aggregation.
  • The findings offer new insights into protein misfolding pathways and potential therapeutic targets.