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 |
| Publication status | Published - 1999 Aug 6 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Spectroscopy
- Atomic and Molecular Physics, and Optics
Cite this
α -Helix propensities of homo-oligomers in aqueous solution studied by multicanonical algorithm. / Mitsutake, Ayori; Okamoto, Yuko.
In: Chemical Physics Letters, Vol. 309, No. 1-2, 06.08.1999, p. 95-100.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - α -Helix propensities of homo-oligomers in aqueous solution studied by multicanonical algorithm
AU - Mitsutake, Ayori
AU - Okamoto, Yuko
PY - 1999/8/6
Y1 - 1999/8/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0002252462&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0002252462&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0002252462
VL - 309
SP - 95
EP - 100
JO - Chemical Physics Letters
JF - Chemical Physics Letters
SN - 0009-2614
IS - 1-2
ER -