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Related Concept Videos

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...
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...
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...
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,...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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Characterizing the cooperativity in H-bonded amino structures.

Tanja van Mourik1, Andrew J Dingley

  • 1Chemistry Department, University College London, 20 Gordon Street, London WC1H 0AJ, U.K. tanja.vanmourik@st-andrews.ac.uk

The Journal of Physical Chemistry. A
|August 7, 2007
PubMed
Summary

Hydrogen bond cooperativity significantly impacts Nuclear Magnetic Resonance (NMR) parameters in G-quartets and cyanamide structures. These changes are driven by electron redistribution as more hydrogen-bonding monomers are added.

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Area of Science:

  • Computational Chemistry
  • Quantum Chemistry
  • Biophysical Chemistry

Background:

  • Hydrogen bonding plays a crucial role in molecular structure and function.
  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for probing molecular structure and dynamics.
  • Understanding cooperative effects in molecular assemblies is essential for predicting their properties.

Purpose of the Study:

  • To investigate the influence of hydrogen bond cooperativity on NMR chemical shifts and spin-spin coupling constants.
  • To analyze these effects in G-quartet and cyanamide monomer assemblies.
  • To elucidate the underlying electronic mechanisms responsible for the observed NMR parameter changes.

Main Methods:

  • Density Functional Theory (DFT) calculations were employed.
  • NMR parameters (chemical shifts and coupling constants) were computed for various G-quartet and cyanamide structures.
  • Calculations were performed on complete assemblies and their fragments to isolate cooperative effects.

Main Results:

  • The magnitude of |1JNH| coupling, 1H and 15N chemical shifts for H-bonding N-H groups, and |h2JNN| H-bond coupling increased with monomer addition.
  • |1JNH| coupling for non-H-bonded N-H groups decreased in magnitude.
  • These changes were observed in both ring and chain structures, with identical monomer geometries in some cases.

Conclusions:

  • Hydrogen bond cooperativity demonstrably alters NMR parameters in G-quartets and cyanamide systems.
  • Electron redistribution due to neighboring H-bonding molecules is the primary cause of these alterations.
  • The findings provide insights into the electronic communication within hydrogen-bonded networks.