Thermodynamics and kinetics of a Go(o)over-bar proteinlike heteropolymer model with two-state folding characteristics

Anna Kallias; Michael Bachmann; Wolfhard Janke

doi:10.1063/1.2822287

Thermodynamics and kinetics of a Go(o)over-bar proteinlike heteropolymer model with two-state folding characteristics

Anna Kallias, Michael Bachmann, Wolfhard Janke

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

Abstract

We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar G (o) over bar -like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force.

Original language	English
Pages (from-to)	055102-7 pp
Journal	Journal of Chemical Physics
Volume	128
Issue number	5
DOIs	https://doi.org/10.1063/1.2822287
Publication status	Published - 2008

Subject classification (UKÄ)

Biophysics

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10.1063/1.2822287

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title = "Thermodynamics and kinetics of a Go(o)over-bar proteinlike heteropolymer model with two-state folding characteristics",

abstract = "We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar G (o) over bar -like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force.",

author = "Anna Kallias and Michael Bachmann and Wolfhard Janke",

year = "2008",

doi = "10.1063/1.2822287",

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publisher = "American Institute of Physics (AIP)",

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T1 - Thermodynamics and kinetics of a Go(o)over-bar proteinlike heteropolymer model with two-state folding characteristics

AU - Kallias, Anna

AU - Bachmann, Michael

AU - Janke, Wolfhard

PY - 2008

Y1 - 2008

N2 - We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar G (o) over bar -like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force.

AB - We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar G (o) over bar -like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force.

U2 - 10.1063/1.2822287

DO - 10.1063/1.2822287

M3 - Article

SN - 0021-9606

VL - 128

SP - 55102

EP - 55107

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

IS - 5

ER -

Thermodynamics and kinetics of a Go(o)over-bar proteinlike heteropolymer model with two-state folding characteristics

Abstract

Subject classification (UKÄ)

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