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 | |
| Publication status | Published - 2003 Apr 15 |
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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 journal › Article
}
TY - JOUR
T1 - Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog
T2 - Diagonal force constants
AU - Ham, Sihyun
AU - Cho, Minhaeng
PY - 2003/4/15
Y1 - 2003/4/15
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=0038637862&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038637862&partnerID=8YFLogxK
U2 - 10.1063/1.1559681
DO - 10.1063/1.1559681
M3 - Article
AN - SCOPUS:0038637862
VL - 118
SP - 6915
EP - 6922
JO - Journal of Chemical Physics
JF - Journal of Chemical Physics
SN - 0021-9606
IS - 15
ER -