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Related Concept Videos

Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

201
The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
201
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

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Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
258

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Related Experiment Video

Updated: Sep 28, 2025

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
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Manipulating Cation-π Interactions with Genetically Encoded Tryptophan Derivatives.

Hongxia Zhao1, Chao Liu1, Wenlong Ding1

  • 1Zhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou 310058, China.

Journal of the American Chemical Society
|April 5, 2022
PubMed
Summary

Researchers enhanced cation-π interactions, crucial for molecular recognition, by using genetically encoded 6-methoxy-tryptophan. This significantly boosted binding affinity for histone H3K4me3 detection and imaging applications.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Molecular Biology

Background:

  • Cation-π interactions are fundamental noncovalent forces in molecular recognition within chemistry and biology.
  • Existing methods struggle to design and synthesize significantly stronger cation-π interactions.

Purpose of the Study:

  • To develop a strategy for enhancing cation-π interaction binding energy.
  • To engineer a high-affinity reader for histone H3K4me3 using genetic code expansion.

Main Methods:

  • Employed genetic code expansion to replace tryptophan (Trp) with an electron-rich derivative (6-methoxy-Trp) in an aromatic box.
  • Systematically engineered the system to create an H3K4me3 Super-Reader.

Main Results:

  • Achieved an eightfold increase in binding affinity between histone H3K4me3 and its reader using genetically encoded 6-methoxy-Trp.
  • Developed an H3K4me3 Super-Reader with single-digit nanomolar affinity for detection and imaging.

Conclusions:

  • The genetic code expansion strategy effectively enhances cation-π interactions.
  • This approach offers a versatile platform for manipulating cation-π interactions in diverse applications, including sensitive biomarker detection.