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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.
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Noncovalent Attractions in Biomolecules02:35

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Typical aromatic noncovalent interactions in proteins: A theoretical study using phenylalanine.

Cherumuttathu H Suresh1, Neetha Mohan, K Periya Vijayalakshmi

  • 1Computational Modeling and Simulation Section, National Institute for Interdisciplinary Science and Technology, Trivandrum. sureshch@gmail.com

Journal of Computational Chemistry
|November 28, 2008
PubMed
Summary

This study investigated noncovalent interactions in phenylalanine complexes, finding cation-pi interactions strongest and CH-pi weakest. Cationic phenylalanine exhibited the most interactions, with varying cooperativity effects observed.

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Area of Science:

  • Computational Chemistry
  • Molecular Interactions
  • Quantum Chemistry

Background:

  • Noncovalent interactions are crucial in molecular recognition and biological systems.
  • Phenylalanine, an amino acid, participates in various intermolecular forces.
  • Understanding these interactions requires accurate theoretical methods.

Purpose of the Study:

  • To systematically investigate CH...pi, OH...pi, NH...pi, and cation...pi interactions in phenylalanine complexes.
  • To evaluate the performance of different theoretical levels for studying these noncovalent interactions.
  • To analyze the cooperativity and strength of these interactions in various phenylalanine forms.

Main Methods:

  • Utilized B3LYP, MP2, MPWB1K, and M06-2X levels of theory.
  • Employed complexes of phenylalanine (cationic, anionic, neutral, zwitterionic) with CH(4), H(2)O, NH(3), and NH(4)(+).
  • Identified noncovalent interactions using electron density at bond critical points (bcps).

Main Results:

  • Cation...pi interactions were strongest (36-46 kcal/mol), followed by OH...pi and NH...pi (6-27 kcal/mol), and CH...pi (0.62-2.55 kcal/mol).
  • Cationic phenylalanine showed the highest interaction strengths across all methods.
  • MPWB1K and M06-2X levels demonstrated superior performance for noncovalent interactions compared to B3LYP.

Conclusions:

  • Cation...pi interactions dominate among the studied forces in phenylalanine complexes.
  • The choice of theoretical method significantly impacts the accuracy of noncovalent interaction studies.
  • MPWB1K and M06-2X are recommended for reliable investigations of weak molecular interactions.