MersV1, Main, Exploration, bibRecordById, pubmed:9502320

A free energy analysis by unfolding applied to 125-mers on a cubic lattice.

Identifieur interne : 003A22 ( Main/Exploration ); précédent : 003A21; suivant : 003A23

A free energy analysis by unfolding applied to 125-mers on a cubic lattice.

Auteurs : M S Chung [États-Unis] ; A F Neuwald ; W J Wilbur

Source :

Folding & design [ 1359-0278 ] ; 1998.

RBID : pubmed:9502320

Descripteurs français

KwdFr :
- Chaines de Markov, Dénaturation des protéines, Modèles chimiques, Pliage des protéines.
MESH :
- Chaines de Markov, Dénaturation des protéines, Modèles chimiques, Pliage des protéines.

English descriptors

KwdEn :
- Markov Chains, Models, Chemical, Protein Denaturation, Protein Folding.
MESH :
- Markov Chains, Models, Chemical, Protein Denaturation, Protein Folding.

Abstract

A common approach to the protein folding problem involves computer simulation of folding using lattice models of amino acid sequences. Key factors for good performance in such models are the correct choice of the temperature and the average interaction energy between residues. In order to push the lattice approach to its limit it is important to have a method to adjust these parameters for optimal folding that is not limited by our ability to successfully simulate folding in a reasonable time.

DOI: 10.1016/S1359-0278(98)00008-X
PubMed: 9502320

Affiliations:

Le document en format XML

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<author><name sortKey="Chung, M S" sort="Chung, M S" uniqKey="Chung M" first="M S" last="Chung">M S Chung</name>
<affiliation wicri:level="2"><nlm:affiliation>National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894</wicri:regionArea>
<placeName><region type="state">Maryland</region>
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<author><name sortKey="Neuwald, A F" sort="Neuwald, A F" uniqKey="Neuwald A" first="A F" last="Neuwald">A F Neuwald</name>
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<author><name sortKey="Wilbur, W J" sort="Wilbur, W J" uniqKey="Wilbur W" first="W J" last="Wilbur">W J Wilbur</name>
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<series><title level="j">Folding & design</title>
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<front><div type="abstract" xml:lang="en">A common approach to the protein folding problem involves computer simulation of folding using lattice models of amino acid sequences. Key factors for good performance in such models are the correct choice of the temperature and the average interaction energy between residues. In order to push the lattice approach to its limit it is important to have a method to adjust these parameters for optimal folding that is not limited by our ability to successfully simulate folding in a reasonable time.</div>
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A free energy analysis by unfolding applied to 125-mers on a cubic lattice.

A free energy analysis by unfolding applied to 125-mers on a cubic lattice.

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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