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Related Concept Videos

Aromatic Hydrocarbon Cations: Structural Overview01:18

Aromatic Hydrocarbon Cations: Structural Overview

3.2K
Cycloheptatriene is a neutral monocyclic unsaturated hydrocarbon that consists of an odd number of carbon atoms and an intervening sp3 carbon in the ring. The three double bonds in the ring correspond to 6 π electrons, which is a Huckel number, and therefore satisfies the criteria of 4n + 2 π electrons. However, the intervening sp3 carbon disrupts the continuous overlap of p orbitals. As a result, cycloheptatriene is not aromatic.
Removing one hydrogen from the intervening CH2 group...
3.2K
Aromatic Hydrocarbon Anions: Structural Overview01:18

Aromatic Hydrocarbon Anions: Structural Overview

3.1K
Neutral hydrocarbons like cyclopentadiene with an odd number of carbon atoms and one intervening CH2 group in the ring are not aromatic. Cyclopentadiene with 4 π electrons does not satisfy the 4n + 2 π electron rule. Additionally, the intervening CH2 group is sp3 hybridized and lacks a vacant p orbital, thereby interrupting the overlap of p orbitals in a continuous manner and preventing the delocalization of π electrons throughout the ring.
Due to the absence of continuous...
3.1K
Ligand Binding Sites02:40

Ligand Binding Sites

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8.1K
Basicity of Heterocyclic Aromatic Amines01:25

Basicity of Heterocyclic Aromatic Amines

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Heterocyclic amines, where the N atom is a part of an alicyclic system, are similar in basicity to alkylamines. Interestingly, the heterocyclic amine having a nitrogen atom as part of an aromatic ring has much less basicity than its corresponding alicyclic counterpart. For this reason, as presented in Figure 1, piperidine (pKb = 2.8) is significantly more basic than pyridine (pKb = 8.8).
6.4K
Conserved Binding Sites01:49

Conserved Binding Sites

4.7K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.7K
Nucleophilic Aromatic Substitution of Aryldiazonium Salts: Aromatic SN101:14

Nucleophilic Aromatic Substitution of Aryldiazonium Salts: Aromatic SN1

2.3K
Treating arylamines with nitrous acid gives aryldiazonium salts that are effective substrates in nucleophilic aromatic substitution reactions. The diazonio group in these salts can be easily displaced by different nucleophiles, yielding a wide variety of substituted benzenes. The leaving group departs as nitrogen gas, and this easy elimination is the driving force for the substitution reaction.
In the Sandmeyer reaction, for example, the diazonio group is replaced by a chloro, bromo,...
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Related Experiment Video

Updated: Oct 17, 2025

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

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Searching for methyllysine-binding aromatic cages.

Kendra R Vann1, Yashavantha L Vishweshwaraiah2, Nikolay V Dokholyan2,3

  • 1Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO, U.S.A.

The Biochemical Journal
|October 8, 2021
PubMed
Summary
This summary is machine-generated.

Researchers identified new methyllysine readers in the cytoplasm, crucial for understanding non-histone protein signaling. This discovery advances knowledge of cell communication beyond the nucleus.

Keywords:
aromatic cagebindingmethylationstructure

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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Proteomics

Background:

  • Lysine methylation is vital for cell signaling pathways.
  • The role of methyllysine readers in the nucleus is known, but cytoplasmic roles are unclear.
  • Understanding cytoplasmic methyllysine recognition is essential for cell biology.

Purpose of the Study:

  • To identify potential methyllysine reader proteins in the cytoplasm.
  • To explore novel mechanisms of non-histone protein regulation.
  • To expand the understanding of post-translational modifications in cellular signaling.

Main Methods:

  • Utilized the Erebus structural motif-mining algorithm.
  • Analyzed the Protein Data Bank (PDB) database.
  • Applied knowledge of known methyllysine binding mechanisms.

Main Results:

  • Successfully searched for and identified potential methyllysine readers.
  • Developed a novel approach for discovering protein-protein interaction motifs.
  • Provided a foundation for further experimental validation of identified readers.

Conclusions:

  • The study presents a computational method for identifying methyllysine readers.
  • Highlights the potential for significant uncharacterized cytoplasmic methyllysine signaling.
  • Opens new avenues for research into non-histone protein function and regulation.