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

Sihyun Ham, Minhaeng Cho

Research output: Contribution to journalArticle

125 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 languageEnglish
Pages (from-to)6915-6922
Number of pages8
JournalJournal of Chemical Physics
Volume118
Issue number15
DOIs
Publication statusPublished - 2003 Apr 15

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Dipeptides
glycine
Amides
Dimers
Glycine
amides
Conformations
dimers
analogs
Hessian matrices
peptides
Peptides
Molecules
molecules
N-methylacetamide

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics

Cite this

Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog : Diagonal force constants. / Ham, Sihyun; Cho, Minhaeng.

In: Journal of Chemical Physics, Vol. 118, No. 15, 15.04.2003, p. 6915-6922.

Research output: Contribution to journalArticle

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