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Related Concept Videos

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...
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...
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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:13

Protein Organization

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Related Experiment Video

Updated: May 28, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Enzymatic Encoding of Topology in an Intrinsically Disordered Single-Chain Protein.

Joshua Johani1,2, Kristin Eichelberger3, Olga Guskova1

  • 1Leibniz-Institut Für Polymerforschung Dresden e.V., Dresden, Germany.

Angewandte Chemie (International Ed. in English)
|May 26, 2026
PubMed
Summary
This summary is machine-generated.

Enzymatic cross-linking creates compact single-chain nanoparticles from disordered proteins. This method precisely controls topology, forming stable structures with reproducible cavities for advanced material design.

Keywords:
SEC‐SAXSenzymatic cross‐linkingintrinsically disordered proteinssingle‐chain nanoparticlestopology encoding

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Area of Science:

  • Polymer Chemistry
  • Protein Chemistry
  • Biophysics

Background:

  • Controlling the 3D topology of single-chain nanoparticles (SCNPs) is challenging, especially for intrinsically disordered proteins (IDPs) lacking defined secondary structures.
  • Intrinsically disordered proteins present unique challenges for creating stable, topologically controlled nanostructures.

Purpose of the Study:

  • To demonstrate selective enzymatic intramolecular cross-linking for encoding topologically biased interactions in intrinsically disordered proteins.
  • To yield compact SCNPs with reproducible cavity architecture using a model protein system.

Main Methods:

  • Utilized microbial transglutaminase (mTGase) for enzymatic intramolecular cross-linking of bovine beta-casein (β-Cn) surrogate (βNaCn).
  • Employed size exclusion chromatography with quintuple detection (SEC-D5), cross-linking mass spectrometry (XL-MS), molecular dynamics (MD) simulations, and SEC-SAXS for structural analysis.
  • Probed protein cavities using Nile red (NR) fluorescence and SEC-SAXS to analyze guest-induced density redistribution.

Main Results:

  • Sparse, sequence-resolved isopeptide bonds induced reproducible chain collapse without secondary structure formation.
  • Structural analyses revealed a topology with a stable hydrophobic core and flexible disordered loops.
  • Cavity architecture was validated through guest capture experiments, demonstrating controlled topology.

Conclusions:

  • Sparse enzymatic cross-linking can encode and validate topology in disordered single chains.
  • This approach enables covalent folding of intrinsically disordered proteins into well-defined single-chain nanoparticles.
  • Establishes a method for designing SCNPs with reproducible topology and cavity architecture, bridging IDP research and SCNP design.