Abstract
Helix-coil transitions of homo-oligomers in aqueous solution are studied by multicanonical Monte Carlo simulations. The solvation effects are represented by the term that is proportional to the solvent-accessible surface area of the peptides. Homo-oligomers of length 10 are considered for two characteristic amino acids, alanine and glycine, which are helix former and helix breaker, respectively. It is shown that the helix-coil transition temperature for homo-alanine in water is considerably lower than in gas phase. The helix propagation parameter s and nucleation parameter σ for both alanine and glycine are calculated and shown to be in remarkable agreement with experimental results.
| Original language | English |
|---|---|
| Pages (from-to) | 95-100 |
| Number of pages | 6 |
| Journal | Chemical Physics Letters |
| Volume | 309 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 1999 Aug 6 |
ASJC Scopus subject areas
- Physics and Astronomy(all)
- Physical and Theoretical Chemistry
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Mitsutake, A., & Okamoto, Y. (1999). α -Helix propensities of homo-oligomers in aqueous solution studied by multicanonical algorithm. Chemical Physics Letters, 309(1-2), 95-100. https://doi.org/10.1016/S0009-2614(99)00661-2