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Related Concept Videos

Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

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From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding
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From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding

Published on: March 24, 2018

Halogen bonding in halocarbon-protein complexes: a structural survey.

Emilio Parisini1, Pierangelo Metrangolo, Tullio Pilati

  • 1Center for Nano Science and Technology (CNST) of IIT@PoliMI, 70/3, via Pascoli, I-20133 Milan, Italy.

Chemical Society Reviews
|March 3, 2011
PubMed
Summary
This summary is machine-generated.

Halogen bonds, interactions involving halogen atoms, can stabilize small molecule-protein complexes. This review highlights their role in drug design, showing how these bonds influence biological structures.

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Area of Science:

  • * Supramolecular chemistry
  • * Medicinal chemistry
  • * Structural biology

Background:

  • * Halogen bonding is well-established in supramolecular systems and materials science.
  • * Its role in stabilizing small molecule-protein complexes has been less recognized.
  • * Halogen bonds involve halogen-substituted molecules interacting with biological targets.

Purpose of the Study:

  • * To review the role of halogen bonds in stabilizing small molecule-protein complexes.
  • * To provide examples of halogen bonds in biologically relevant systems.
  • * To illustrate the potential of halogen bonds in rational drug design.

Main Methods:

  • * Analysis of crystal structures of small molecule-protein complexes.
  • * Identification of halogen bonding interactions (donor-acceptor pairs).
  • * Examination of diverse compounds including pharmaceuticals and environmental agents.

Main Results:

  • * Demonstrated halogen bonds between halogen-substituted ligands and biological substrates.
  • * Identified iodine, bromine, and chlorine as effective halogen bond donors.
  • * Showcased electron-rich sites (O, N, S, π-systems) as halogen bond acceptors.
  • * Presented crystal structures illustrating these interactions in biological contexts.

Conclusions:

  • * Halogen bonds are significant stabilizing forces in biological systems.
  • * These interactions are directional and can be exploited in drug design.
  • * Understanding halogen bonding can lead to the development of novel therapeutics.