MersV1, Main, Exploration, bibRecord, 003236

3D-Lattice Monte Carlo simulations of model proteins. Size effects on folding thermodynamics and kinetics.

Identifieur interne : 003236 ( Main/Exploration ); précédent : 003235; suivant : 003237

3D-Lattice Monte Carlo simulations of model proteins. Size effects on folding thermodynamics and kinetics.

Auteurs : K. Leonhard [États-Unis] ; J M Prausnitz ; C J Radke

Source :

Biophysical chemistry [ 0301-4622 ] ; 2003.

RBID : pubmed:14516915

Descripteurs français

KwdFr :
- Cinétique, Données de séquences moléculaires, Méthode de Monte-Carlo, Pliage des protéines, Protéines (), Protéines (métabolisme), Séquence d'acides aminés, Température, Thermodynamique.
MESH :
- métabolisme : Protéines.
- Cinétique, Données de séquences moléculaires, Méthode de Monte-Carlo, Pliage des protéines, Protéines, Séquence d'acides aminés, Température, Thermodynamique.

English descriptors

KwdEn :
- Amino Acid Sequence, Kinetics, Molecular Sequence Data, Monte Carlo Method, Protein Folding, Proteins (chemistry), Proteins (metabolism), Temperature, Thermodynamics.
MESH :
- chemical , chemistry : Proteins.
- chemical , metabolism : Proteins.
- Amino Acid Sequence, Kinetics, Molecular Sequence Data, Monte Carlo Method, Protein Folding, Temperature, Thermodynamics.

Abstract

Recently, we devised an energy scale to vary systematically amino-acid residue-solvent interactions for Monte Carlo simulations of lattice-model proteins in water. For 27-mer proteins, the folding behavior varies appreciably with the choice of interaction parameters. We now perform similar simulations with 64-mers to study the size dependence of the optimal energy parameter set for representing realistic behavior typical of many real proteins (i.e. fast folding and high cooperativity for single chains). We find that 64-mers are considerably more stable and more cooperative compared to 27-mers. The optimal interfacial-interaction-energy parameter set, however, is relatively size independent.

DOI: 10.1016/s0301-4622(03)00185-6
PubMed: 14516915

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Recently, we devised an energy scale to vary systematically amino-acid residue-solvent interactions for Monte Carlo simulations of lattice-model proteins in water. For 27-mer proteins, the folding behavior varies appreciably with the choice of interaction parameters. We now perform similar simulations with 64-mers to study the size dependence of the optimal energy parameter set for representing realistic behavior typical of many real proteins (i.e. fast folding and high cooperativity for single chains). We find that 64-mers are considerably more stable and more cooperative compared to 27-mers. The optimal interfacial-interaction-energy parameter set, however, is relatively size independent.</div>
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3D-Lattice Monte Carlo simulations of model proteins. Size effects on folding thermodynamics and kinetics.

3D-Lattice Monte Carlo simulations of model proteins. Size effects on folding thermodynamics and kinetics.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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