Abstract
Ab initio conformational analysis of the dipeptide Ac-Valine-Alanine-NHMe was performed and optimized at the RHF/3-21g level of theory in an attempt to characterize the folding of short peptides. A topological scan of alanine's (Ala) ψ and φ rotors was carried out with valine (Val) in the βL geometry to construct a Ramachandran surface in two- and three-dimensions. It was observed that Val sterically dominates the conformations of Ala. Of the 243 possible conformers in this study, 202 were found. Those that were not found had converged to a different geometry of lower energy and greater stability. The γL and εL conformers of Ala were favoured, and 47 of the found conformers can be classified as potential β-turns according to the traditional backbone torsional definitions. However, the potentially most stable conformer, αDaγL, was not in one of these regions of the Ramachandran surface. Thus, β-turns may not be inherent conformations of the Val-Ala dipeptide, but may arise preferentially within protein structures due to certain steric effects from the surrounding environment.
Original language | English (US) |
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Pages (from-to) | 177-184 |
Number of pages | 8 |
Journal | Journal of Molecular Structure: THEOCHEM |
Volume | 729 |
Issue number | 3 |
DOIs | |
State | Published - Sep 30 2005 |
Keywords
- β-Turn
- Ab initio
- Ac-Valine-Alanine-NHMe
- Dipeptide model
- RHF/3-21G
ASJC Scopus subject areas
- Biochemistry
- Condensed Matter Physics
- Physical and Theoretical Chemistry