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Hydrogen Bonds01:04

Hydrogen Bonds

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A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
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Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
Hydrogen Bonds Control the World!
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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
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Noncovalent Attractions in Biomolecules02:35

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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Electrophiles02:28

Electrophiles

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This lesson explains the definition, classification, and characteristic features of an electrophile that are key features of nucleophilic substitution reactions. An analysis of their charge and orbital picture helps understand their reactivity for seeking electrons. Electrophiles can be classified into positive and neutral species. Other classes include free radicals and polar functional groups.
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From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding
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Halogen Bonds in Protein Nucleic Acid Recognition.

Antonio Frontera1, Antonio Bauzá1

  • 1Department of Chemistry, Universitat de les Illes Balears, Crta. de Valldemossa km 7.5, 07122 Palma, Baleares, Spain.

Journal of Chemical Theory and Computation
|June 25, 2020
PubMed
Summary

Halogenated nucleic acids (NA) can form halogen bonds with proteins, a previously underappreciated interaction. This discovery reveals new insights into molecular recognition and protein-NA binding, crucial for biological processes.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Biology

Background:

  • Molecular recognition and aggregation are vital biological processes.
  • Halogenation of nucleic acids (NA) is common in structural studies.
  • Halogens can participate in noncovalent interactions like halogen bonding.

Purpose of the Study:

  • To investigate the role of halogen bonding in protein-NA interactions.
  • To explore the potential of halogenated NA in molecular recognition.

Main Methods:

  • Analysis of Protein Data Bank (PDB) structures.
  • Computational analysis of halogen bonding interactions.

Main Results:

  • Halogenated NA (with Br or I) form halogen bonds with protein residues.
  • Observed examples in PDB include 5-iodouracil, 5-bromouracil, 8-bromoadenine, and 5-iodocytosine.
  • Computational studies confirm favorable and moderately strong halogen bonding.

Conclusions:

  • Halogenated NA actively participate in protein-NA binding through halogen bonds.
  • This interaction offers new perspectives on molecular recognition in biological systems.