Abstract
The elastic properties of the α-helix of poly-L-glycine have been investigated by means of periodic self-consistent field (SCF) calculations and localized molecular orbitals (LMO), within the framework of the semi-empirical AM1 method. A cluster containing eighteen L-glycine residues was progressively stretched along the main axis and its geometry was re-optimized by fixing only the total length, in order to maintain the α-helix structure at the strained state. From the regression analysis of the calculated heat of formation versus cluster length, we obtained a longitudinal Young's elastic modulus of 65 GPa. The formation of a non-planar peptide bond indicates the appearance of strain localization in the α-helix structure under tensile loading.
Original language | English |
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Pages (from-to) | 536-542 |
Number of pages | 7 |
Journal | Chemical Physics Letters |
Volume | 322 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2000 Jun 2 |
Externally published | Yes |
ASJC Scopus subject areas
- Physics and Astronomy(all)
- Physical and Theoretical Chemistry