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An exploratory ab initio study on the entropy of various backbone conformers for the HCO-Gly-Gly-Gly-NH2tripeptide motif

Journal of Molecular Structure THEOCHEM
Publication Date
DOI: 10.1016/j.theochem.2003.08.016
  • Glycine
  • Tripeptide
  • Entropy
  • Gibbs Free Energy
  • Ab Initio
  • Ramachandran Cross-Section
  • Hco-Gly-Gly-Gly-Nh2
  • Physics


Abstract Ab initio molecular computations were carried out on the HCO-Gly-Gly-Gly-NH 2 tripeptide at the RHF/6-311G(d,p) level of theory. The two terminal glycine moieties were kept in the β l conformations while the conformation of the central glycine was varied. All five minima of the central glycine residue were optimized and in addition to electronic energy ( E), the key thermodynamic functions: enthalpy ( H), Gibbs-free energy ( G) and entropy ( S) were obtained. Cross-sections along each of φ and ψ passing through the fully extended β l conformations, were generated from the Ramachandran Potential Energy Surface and the role of entropy change (Δ S) in the folding process is assessed.

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