Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog: Diagonal force constants

Sihyun Ham; Minhaeng Cho

doi:10.1063/1.1559681

Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog: Diagonal force constants

Sihyun Ham, Minhaeng Cho

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

135 Citations (Scopus)

Abstract

Extensive ab initio vibrational analyses were performed for three series of dimer systems consisting of two trans-NMA molecules varying the intermolecular distance. i.e., α-helical, parallel, and antiparallel β-sheet conformations. Using the Hessian matrix reconstruction method, the local amide I mode frequencies of each peptide and the coupling constants were obtained for a number of NMA dimer and GD conformations.

Original language	English
Pages (from-to)	6915-6922
Number of pages	8
Journal	Journal of Chemical Physics
Volume	118
Issue number	15
DOIs	https://doi.org/10.1063/1.1559681
Publication status	Published - 2003 Apr 15

ASJC Scopus subject areas

Physics and Astronomy(all)
Physical and Theoretical Chemistry

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title = "Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog: Diagonal force constants",

abstract = "Extensive ab initio vibrational analyses were performed for three series of dimer systems consisting of two trans-NMA molecules varying the intermolecular distance. i.e., α-helical, parallel, and antiparallel β-sheet conformations. Using the Hessian matrix reconstruction method, the local amide I mode frequencies of each peptide and the coupling constants were obtained for a number of NMA dimer and GD conformations.",

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AB - Extensive ab initio vibrational analyses were performed for three series of dimer systems consisting of two trans-NMA molecules varying the intermolecular distance. i.e., α-helical, parallel, and antiparallel β-sheet conformations. Using the Hessian matrix reconstruction method, the local amide I mode frequencies of each peptide and the coupling constants were obtained for a number of NMA dimer and GD conformations.

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Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog: Diagonal force constants

Abstract

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