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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Molecules that possess multiple chiral centers can afford a large number of stereoisomers. For instance, while some molecules like 2-butanol have one chiral center, defined as a tetrahedral carbon atom with four different substituents attached, several molecules like butane-2,3-diol have multiple chiral centers. A simple formula to predict the number of stereoisomers possible for a molecule with n chiral centers is 2n. However, there can be a lower number where some of the stereoisomers are...
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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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In Ultraviolet–Visible (UV–Vis) spectroscopy, the absorption of electromagnetic radiation is used to probe the electronic structure of molecules. This technique provides insights into molecular electronic transitions, particularly the movement of electrons between different molecular orbitals. Radiation is absorbed if the energy of the electromagnetic radiation passing through the molecule is precisely equal to the energy difference between the excited and ground states. During this process,...

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Chiroptical switching in a bistable molecular shuttle.

Giovanni Bottari1, David A Leigh, Emilio M Pérez

  • 1School of Chemistry, University of Edinburgh, The King's Buildings, West Mains Road, Edinburgh EH9 3JJ, UK.

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|October 30, 2003
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Researchers developed a novel chiroptical switch using rotaxane molecular shuttles. Light triggers macrocycle movement, creating a strong circular dichroism signal when bound to a chiral peptide.

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Area of Science:

  • Supramolecular Chemistry
  • Molecular Machines
  • Chiroptical Spectroscopy

Background:

  • Bistable rotaxane-based molecular shuttles enable controlled movement of macrocycles.
  • Exploiting molecular motion to induce property changes remains an underexplored area.

Purpose of the Study:

  • To demonstrate a property change triggered by controlled large-amplitude translational motion in a rotaxane.
  • To develop a novel chiroptical switch based on rotaxane functionality.

Main Methods:

  • Synthesis of a [2]rotaxane with a specific thread and macrocycle.
  • Utilizing light to induce translational motion of the macrocycle.
  • Investigating the chiroptical response (induced circular dichroism) under different conditions.

Main Results:

  • Achieved light-induced, large-amplitude translational motion of the macrocycle along the rotaxane thread.
  • Observed a strong induced circular dichroism (ICD) response.
  • The ICD response was highly dependent on the macrocycle's interaction with a chiral peptide station via hydrogen bonding.

Conclusions:

  • Demonstrated the first example of a property change driven by controlled translational motion in a rotaxane.
  • Successfully designed a novel chiroptical switch with light-controllable functionality.
  • The switch's performance is modulated by specific molecular recognition events (hydrogen bonding to a chiral peptide).