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Related Concept Videos

Amino acids03:42

Amino acids

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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...
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Allosteric Proteins-ATCase01:19

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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tRNA Activation02:26

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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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...
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Amino Acid Catabolism01:18

Amino Acid Catabolism

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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...
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Related Experiment Video

Updated: Jan 11, 2026

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

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Twinned l-aspartic acid.

Martin Lutz1

  • 1Structural Biochemistry, Bijvoet Centre for Biomolecular Research, Faculty of Science, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands.

Iucrdata
|November 12, 2025
PubMed
Summary
This summary is machine-generated.

This study reveals asymmetric double-well hydrogen bonds in carboxylate groups by enhancing data quality and twin handling during intensity integration. These findings are supported by crystallographic refinements using both spherical and non-spherical scattering factors.

Keywords:
hydrogen bondingnon-spherical scattering factorsraw datatwinning

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Area of Science:

  • Crystallography
  • Chemical Physics

Background:

  • Accurate crystallographic data is crucial for understanding molecular interactions.
  • Hydrogen bonds play a significant role in molecular structure and function.
  • Distinguishing between different hydrogen bond types requires high-quality structural data.

Purpose of the Study:

  • To investigate the nature of hydrogen bonds between carboxylate groups in the title molecule.
  • To improve the quality of crystallographic data through advanced twin handling techniques.
  • To determine if asymmetric double-well hydrogen bonds are present.

Main Methods:

  • Improving crystallographic data quality via appropriate twin handling in intensity integration.
  • Analyzing difference-Fourier maps to identify structural features.
  • Performing crystallographic refinements using both Independent Atom Model (IAM) spherical scattering factors and Non-spherical Atomic Scattering Factors (NoSpherA2).

Main Results:

  • Enhanced data quality revealed indications of asymmetric double-well hydrogen bonds.
  • Difference-Fourier maps provided evidence supporting the presence of these specific hydrogen bonds.
  • Crystallographic refinements using both IAM and NoSpherA2 scattering factors were consistent with the observed hydrogen bond geometry.

Conclusions:

  • The study successfully identified asymmetric double-well hydrogen bonds between carboxylate groups.
  • Advanced data processing techniques, including twin handling, are essential for accurate structural determination.
  • The findings contribute to a better understanding of hydrogen bonding in crystalline materials.