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.

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	33-43
Number of pages	11
Journal	Journal of Molecular Structure: THEOCHEM
Volume	370
Issue number	1
DOIs	https://doi.org/10.1016/S0166-1280(96)04745-8
Publication status	Published - 10 Oct 1996
Externally published	Yes

Keywords

Continuum solvation model
Helix stability
Monte carlo dynamics
Peptide conformation
Protein folding

IMC Research Focuses

Medical biotechnology

ÖFOS 2012 - Austrian Fields of Study

104022 Theoretical chemistry
104004 Chemical biology
304005 Medical biotechnology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/S0166-1280(96)04745-8

Cite this

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title = "Influence of solvation on helix formation of poly-alanine studied by multiple annealing simulations",

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",

year = "1996",

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doi = "10.1016/S0166-1280(96)04745-8",

language = "English",

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pages = "33--43",

journal = "Journal of Molecular Structure: THEOCHEM",

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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

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

M3 - Article

AN - SCOPUS:0007397506

SN - 0166-1280

VL - 370

SP - 33

EP - 43

JO - Journal of Molecular Structure: THEOCHEM

JF - Journal of Molecular Structure: THEOCHEM

IS - 1

ER -

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

Abstract

Keywords

IMC Research Focuses

ÖFOS 2012 - Austrian Fields of Study

UN SDGs

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