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Related Concept Videos

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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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
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Chirality at Nitrogen, Phosphorus, and Sulfur02:30

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Chirality is most prevalent in carbon-based tetrahedral compounds, but this important facet of molecular symmetry extends to sp3-hybridized nitrogen, phosphorus and sulfur centers, including trivalent molecules with lone pairs. Here, the lone pair behaves as a functional group in addition to the other three substituents to form an analogous tetrahedral center that can be chiral.
A consequence of chirality is the need for enantiomeric resolution. While this is theoretically possible for all...
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Hybridization of Atomic Orbitals II03:35

Hybridization of Atomic Orbitals II

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sp3d and sp3d 2 Hybridization
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Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
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Updated: Aug 25, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
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Interplay between hydrogen and chalcogen bonds in cysteine.

Oliviero Carugo1,2

  • 1Department of Chemistry, University of Pavia, Pavia, Italy.

Proteins
|October 17, 2022
PubMed
Summary

Cysteine

Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Biology

Background:

  • Protein structures rely on chemical interactions between amino acids.
  • Cysteine's thiol group can form both hydrogen bonds and chalcogen bonds.
  • These interactions can compete, influencing protein stability.

Purpose of the Study:

  • To investigate the competition between hydrogen bonds and chalcogen bonds involving cysteine.
  • To analyze the prevalence and interplay of these bonds in protein structures.

Main Methods:

  • Survey of the Protein Data Bank (PDB) for bond interactions involving cysteine.
  • Analysis of bonding patterns and frequencies.

Main Results:

  • Hydrogen bonds are significantly more common (40-50 times) than chalcogen bonds involving cysteine.
Keywords:
Protein Data Bankchalcogen bondhydrogen bondprotein structure

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  • Despite lower frequency, chalcogen bonds are observed, sometimes concurrently with hydrogen bonds.
  • Cysteine thiol groups forming chalcogen bonds often act as hydrogen bond donors.

    • Conclusions:

    • Hydrogen bonds are generally more prevalent than chalcogen bonds, suggesting they are often stronger.
    • Cysteine can participate in multiple bonding interactions simultaneously.
    • Understanding these competing interactions is crucial for predicting and stabilizing protein structures.