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Peptide models XI. Substitution effects on peptide chains. The magnitude of side-chain–backbone interactions in oligopeptides HCO-(NHCHRCO)<i>n</i>-NH<sub>2</sub> for R=CH<sub>3</sub>. An ab initio study
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Citations
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References
1995
Year
HalogenationOligopeptide ConformationsBiochemistryNatural SciencesPeptide LibraryHydrogen BondMolecular BiologyPeptide Models XiPeptide SynthesisOrganic ChemistryPeptide ScienceReaction IntermediateChemistryOligopeptides Hco-Chemical BiologyPeptide ChainsStabilization EffectStabilization Energy
The stabilization effect of the Me group with respect to H has been determined for peptides of the type HCO-(NH-CHR-CO) n -NH 2 for 1 ≤ n ≤ 3. It was found that for the Me group the stabilization energy was in the vicinity of 5.4 kcal/mol. The site of substitution had no appreciable effect on the stabilization energy. The stabilization energy for monomethyl substitution (R=CH 3 ) ranged from 5.21 to 5.60 kcal/mol. For dimethyl substitution the values were between 10.53 and 10.81 kcal/mol, and for trimethyl substitution it was 15.99 kcal/mol. Keywords: stabilization effects of substituents, oligopeptide conformations, ab initio study on HCO-(NHCHRCO) n -NH 2 .
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