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Amino acids

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...

Amino Acid Catabolism

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...

Amino Acid Biosynthetic Pathways

Amino Acid Biosynthetic Pathways

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...

Lewis Acids and Bases

Lewis Acids and Bases

In 1923, G. N. Lewis proposed a generalized definition of acid-base behavior in which acids and bases are identified by their ability to accept or to donate a pair of electrons and form a coordinate covalent bond.
A coordinate covalent bond (or dative bond) occurs when one of the atoms in the bond provides both bonding electrons. For example, a coordinate covalent bond occurs when a water molecule combines with a hydrogen ion to form a hydronium ion. A coordinate covalent bond also results when...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Ions as Acids and Bases

Ions as Acids and Bases

Salts with Acidic Ions
Salts are ionic compounds composed of cations and anions, either of which may be capable of undergoing an acid or base ionization reaction with water. Aqueous salt solutions, therefore, may be acidic, basic, or neutral, depending on the relative acid-base strengths of the salt’s constituent ions. For example, dissolving the ammonium chloride in water results in its dissociation, as described by the equation:

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Related Experiment Video

Updated: Feb 4, 2026

Bioorthogonal Chemical Imaging of Cell Metabolism Regulated by Aromatic Amino Acids

Bioorthogonal Chemical Imaging of Cell Metabolism Regulated by Aromatic Amino Acids

Published on: May 12, 2023

Programmable Multicomponent Self-Assembly Based on Aromatic Amino Acids.

Pengyao Xing¹, Soo Zeng Fiona Phua¹, Xuan Wei¹

¹Division of Chemistry and Biological Chemistry, School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Singapore.

Advanced Materials (Deerfield Beach, Fla.)

|October 11, 2018

Summary

This summary is machine-generated.

Researchers developed a new method for creating ordered self-assemblies using aromatic amino acids. This hydrogen-bonding driven coassembly avoids complex host-guest interactions, enabling programmable structures.

Keywords:

aromatic amino acids hydrogen bonding multicomponent self-assembly superchirality ternary coassembly

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Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers

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Published on: June 24, 2019

Area of Science:

Supramolecular Chemistry
Organic Chemistry
Materials Science

Background:

Constructing ordered self-assemblies from multiple organic building blocks is complex due to competing pathways.
Existing methods often rely on metal-ligand or host-guest interactions, limiting design flexibility.

Purpose of the Study:

To develop a strategy for integrating aromatic amino acids into multi-component coassemblies.
To achieve ordered structures driven by hydrogen bonding, bypassing traditional complexation methods.

Main Methods:

Utilized a C3-symmetric molecule with alternating hydrogen bond donor/acceptor sites.
Incorporated carboxylic acid or pyridine appended building units, including aromatic amino acids and bipyridine.
Investigated coassembly pathways through pairwise and ternary interactions.

Main Results:

Successfully formed two- and three-component coassemblies driven by hydrogen bonding.
Demonstrated that aromatic amino acids can be programmed via substituents at the alpha-position.
Unveiled three distinct coassembly pathways: two pairwise and one ternary combination.

Conclusions:

Aromatic amino acids can be effectively integrated into hydrogen-bonding driven coassemblies.
This approach offers a programmable route to complex, ordered supramolecular structures.
The strategy provides a versatile platform for designing novel organic materials.