Influence of solvation on helix formation of poly-alanine studied by multiple annealing simulations

The influence of solvation on α-helix formation is studied for a 14-residue homoalanine and a 16-residue alanine-based polypeptide, in aqueous solution. Four variants of Dynamic Monte Carlo (DMC) simulations, using a multiple annealing procedure are performed. The results obtained under in vacuo con...

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Bibliographic Details
Published inJournal of molecular structure. Theochem Vol. 370; no. 1; pp. 33 - 43
Main Authors Klein, Christian Th, Mayer, Bernd, Köhler, Gottfried, Wolschann, Peter
Format Journal Article
LanguageEnglish
Published Elsevier B.V 10.10.1996
Subjects
Continuum solvation model
Helix stability
Monte Carlo dynamics
Peptide conformation
Protein folding
Continuum solvation model
Peptide conformation
Monte Carlo dynamics
Helix stability
Protein folding
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Summary:The influence of solvation on α-helix formation is studied for a 14-residue homoalanine and a 16-residue alanine-based polypeptide, in aqueous solution. Four variants of Dynamic Monte Carlo (DMC) simulations, using a multiple annealing procedure are performed. The results obtained under in vacuo conditions are compared to simulations considering either contributions to the solvation energy of non-favourable solvent interactions by hydrophobic groups, or the total solvation energy, both calculated by a continuum approximation. The highest average helix lengths are found when the total solvation energy (hydrophilic and hydrophobic contributions) is considered, although solvation counteracts the formation of compact peptide structures. The influence of solvation on helix formation is discussed.
ISSN:0166-1280
1872-7999
DOI:10.1016/S0166-1280(96)04745-8