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

Christian Th Klein; Bernd Mayer; Gottfried Köhler; Peter Wolschann

doi:10.1016/S0166-1280(96)04745-8

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

Christian Th Klein, Bernd Mayer, Gottfried Köhler, Peter Wolschann

Inst. Theor. Chem. Strahlenchemie U.

Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

Abstract

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.

Originalsprache	Englisch
Seiten (von - bis)	33-43
Seitenumfang	11
Fachzeitschrift	Journal of Molecular Structure: THEOCHEM
Jahrgang	370
Ausgabenummer	1
DOIs	https://doi.org/10.1016/S0166-1280(96)04745-8
Publikationsstatus	Veröffentlicht - 10 Okt. 1996
Extern publiziert	Ja

IMC Forschungsschwerpunkte

Medical biotechnology

ÖFOS 2012 - Österreichischen Systematik der Wissenschaftszweige

104022 Theoretische Chemie
104004 Chemische Biologie
304005 Medizinische Biotechnologie

UN SDGs

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10.1016/S0166-1280(96)04745-8

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abstract = "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.",

keywords = "Continuum solvation model, Helix stability, Monte carlo dynamics, Peptide conformation, Protein folding",

author = "Klein, {Christian Th} and Bernd Mayer and Gottfried K{\"o}hler and Peter Wolschann",

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T1 - Influence of solvation on helix formation of poly-alanine studied by multiple annealing simulations

AU - Klein, Christian Th

AU - Mayer, Bernd

AU - Köhler, Gottfried

AU - Wolschann, Peter

PY - 1996/10/10

Y1 - 1996/10/10

N2 - 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.

AB - 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.

KW - Continuum solvation model

KW - Helix stability

KW - Monte carlo dynamics

KW - Peptide conformation

KW - Protein folding

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U2 - 10.1016/S0166-1280(96)04745-8

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

Abstract

IMC Forschungsschwerpunkte

ÖFOS 2012 - Österreichischen Systematik der Wissenschaftszweige

UN SDGs

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