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Related Concept Videos

Protein Organization01:24

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Updated: Sep 11, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Localized Hydrolysis-Based Proximity Reporting Platform for Protein Hierarchical Structure Profiling.

Wei Li1, Yiran Li1, Nan Wang1

  • 1State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.

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|August 19, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed a localized hydrolysis-based proximity reporting (LHPR) platform to image glycans on proteins. This tool uses New Delhi metallo-beta-lactamase 1 (NDM-1) for precise, proximity-dependent analysis of glycoprotein architecture.

Keywords:
Fluorescence probeGlycanHierarchical structureProximity activationβ‐Lactamase

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Molecular Biology

Background:

  • Hydrolases offer unique strategies for engineering controllable molecular switches.
  • Spatial proximity information can be transmitted via localized hydrolysis between distinct biomolecular hierarchies, such as proteins and glycans.

Purpose of the Study:

  • To develop a localized hydrolysis-based proximity reporting (LHPR) platform for in situ elucidation of glycoprotein hierarchical architecture.
  • To enable protein-specific imaging of glycans using programmed enzyme activity.

Main Methods:

  • Utilized New Delhi metallo-beta-lactamase 1 (NDM-1) as the core enzyme for the LHPR platform.
  • Constructed protein probes by conjugating target-recognizing molecules with NDM-1.
  • Designed click chemistry-reactive, substrate-caged fluorescent molecules as glycan probes for proximity-dependent activation.

Main Results:

  • Demonstrated in situ protein-specific imaging of glycans within various biological specimens.
  • Successfully quantified distinct glycans of individual proteins using the LHPR platform.
  • Established the principle of protein-specific glycosylation stoichiometry analysis within a unified enzymatic framework.

Conclusions:

  • The LHPR platform provides a powerful tool for analyzing glycoprotein architecture.
  • This technology offers new possibilities for developing glycoprotein-based disease biomarkers, therapeutic targets, and diagnostic approaches.
  • The findings advance precision medicine research through enhanced understanding of glycoproteins.