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Related Concept Videos

Prochirality02:05

Prochirality

The concept of prochirality leads to the nomenclature of the individual faces of a molecule and plays a crucial role in the enantioselective reaction. It is a concept where two or more achiral molecules react to produce chiral products. A typical process is the reaction of an achiral ketone to generate a chiral alcohol. Here, the achiral reactant reacts with an achiral reducing agent, sodium borohydride, to generate an equimolar mixture of the chiral enantiomers of the product. For example, an...
Chirality at Nitrogen, Phosphorus, and Sulfur02:30

Chirality at Nitrogen, Phosphorus, and Sulfur

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...
Chirality in Nature02:30

Chirality in Nature

Chirality is the most intriguing yet essential facet of nature, governing life’s biochemical processes and precision. It can be observed from a snail shell pattern in a macroscopic world to an amino acid, the minutest building block of life. Most of the snails around the world have right-coiled shells because of the intrinsic chirality in their genes. All the amino acids present in the human body exist in an enantiomerically pure state, except for glycine - the sole achiral amino acid. The...
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Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Chirality02:25

Chirality

Chirality is a term that describes the lack of mirror symmetry in an object. In other words, chiral objects cannot be superposed on their mirror images. For example, our feet are chiral, as the mirror image of the left foot, the right foot, cannot be superposed on the left foot.
Chiral objects exhibit a sense of handedness when they interact with another chiral object. For example, our left foot can only fit in the left shoe and not in the right shoe. Achiral objects — objects that have...

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Related Experiment Video

Updated: May 19, 2026

Construction and Systematical Symmetric Studies of a Series of Supramolecular Clusters with Binary or Ternary Ammonium Triphenylacetates
06:35

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Published on: February 15, 2016

Chirality and packing in small proline clusters.

Natalya Atlasevich1, Alison E Holliday, Stephen J Valentine

  • 1Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.

The Journal of Physical Chemistry. B
|August 25, 2012
PubMed
Summary
This summary is machine-generated.

Proline clusters show varying chiral preferences based on size. Packing efficiency influences whether homochiral or mixed-chirality proline assemblies are more stable, offering insights into the origin of biological chirality.

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Area of Science:

  • Biophysical Chemistry
  • Chemical Physics
  • Origin of Life Studies

Background:

  • Chirality is fundamental to biological systems.
  • The origin of homochirality in biomolecules remains a key question.
  • Amino acid clusters are potential precursors to biologically relevant molecules.

Purpose of the Study:

  • To investigate the gas-phase structures and chiral preferences of proline clusters.
  • To understand how cluster size and composition affect stability and packing.
  • To explore the role of proline cluster assembly in the context of homochirality.

Main Methods:

  • Ion mobility/mass spectrometry techniques were employed.
  • Singly charged proline clusters (2-6 monomers) were analyzed.
  • Deuterated L-proline and varying enantiopure to racemic solutions were used to probe cluster composition.

Main Results:

  • [2Pro+H](+) and [3Pro+H](+) clusters showed similar collision cross sections for homochiral and heterochiral assemblies.
  • [4Pro+H](+) and [6Pro+H](+) clusters exhibited smaller collision cross sections for homochiral clusters, indicating a preference for homochirality.
  • [5Pro+H](+) clusters displayed a preference for heterochirality, with smaller collision cross sections for heterochiral compositions.

Conclusions:

  • Cluster packing efficiency significantly influences the stability of proline multimers.
  • Proline cluster assembly can favor either homochiral or mixed-chirality states.
  • These findings provide insights into the self-assembly processes relevant to the origin of biological homochirality.