Peptide models. XIV. Ab initio study on the role of side-chain backbone interaction stabilizing the building unit of right- and left-handed helices in peptides and proteins

1997 ◽  
Vol 61 (5) ◽  
pp. 797-814 ◽  
Author(s):  
Andr�s Perczel ◽  
�d�n Farkas ◽  
John F. Marcoccia ◽  
Imre G. Csizmadia
Keyword(s):  
Ab Initio ◽  
Side Chain ◽  
Ab Initio Study ◽  
Building Unit ◽  
Left Handed ◽  
Peptide Models

Peptide models XI. Substitution effects on peptide chains. The magnitude of side-chain–backbone interactions in oligopeptides HCO-(NHCHRCO)n-NH2 for R=CH3. An ab initio study

1995 ◽  
Vol 73 (10) ◽  
pp. 1563-1572 ◽  
Author(s):  
M.A. McAllister ◽  
G. Endredi ◽  
J. Ladik ◽  
W. Viviani ◽  
A. Perczel ◽  
...  
Keyword(s):  
Ab Initio ◽  
Stabilization Energy ◽  
Side Chain ◽  
Substitution Effects ◽  
Appreciable Effect ◽  
Ab Initio Study ◽  
Peptide Models ◽  
Stabilization Effect

The stabilization effect of the Me group with respect to H has been determined for peptides of the type HCO-(NH-CHR-CO)n-NH2 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=CH3) 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-NH2.

An ab initio study of the side chain of Nafion

2004 ◽  
Vol 389 (1-3) ◽  
pp. 64-67 ◽  
Author(s):  
Yasuharu Okamoto
Keyword(s):  
Ab Initio ◽  
Side Chain ◽  
Ab Initio Study
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