α -Helix propensities of homo-oligomers in aqueous solution studied by multicanonical algorithm

Ayori Mitsutake, Yuko Okamoto

Research output: Contribution to journalArticle

17 Citations (Scopus)

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 languageEnglish
Pages (from-to)95-100
Number of pages6
JournalChemical Physics Letters
Volume309
Issue number1-2
Publication statusPublished - 1999 Aug 6
Externally publishedYes

Fingerprint

oligomers
Oligomers
Alanine
helices
aqueous solutions
alanine
Glycine
glycine
Solvation
coils
Nucleation
Gases
circuit breakers
Amino Acids
Peptides
Water
peptides
solvation
amino acids
transition temperature

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 journalArticle

Mitsutake, Ayori ; Okamoto, Yuko. / α -Helix propensities of homo-oligomers in aqueous solution studied by multicanonical algorithm. In: Chemical Physics Letters. 1999 ; Vol. 309, No. 1-2. pp. 95-100.
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