Hunting for "key residues" in the modeling of globular protein folding: an artificial neural network-based approach.
Identifieur interne : 002010 ( Main/Exploration ); précédent : 002009; suivant : 002011Hunting for "key residues" in the modeling of globular protein folding: an artificial neural network-based approach.
Auteurs : Roberto Sacile [Italie] ; Carmelina RuggieroSource :
- IEEE transactions on nanobioscience [ 1536-1241 ] ; 2002.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acids (chemistry), Amino Acids (classification), Computer Simulation, Models, Chemical, Models, Molecular, Molecular Sequence Data, Neural Networks (Computer), Pattern Recognition, Automated (methods), Protein Conformation, Protein Folding, Proteins (chemistry), Proteins (classification), Sequence Analysis, Protein.
- MESH :
- chemical , chemistry : Amino Acids, Proteins.
- chemical , classification : Amino Acids, Proteins.
- methods : Pattern Recognition, Automated.
- Amino Acid Sequence, Computer Simulation, Models, Chemical, Models, Molecular, Molecular Sequence Data, Neural Networks (Computer), Protein Conformation, Protein Folding, Sequence Analysis, Protein.
Abstract
An approach to modeling globular protein folding based on artificial neural networks (ANNs) is presented. This approach, that can be regarded as an inverse protein folding problem, investigates whether and when a protein fragment needs a specific residue in the center of its primary structure as a necessary condition to fold as observed. To perform this analysis, an ANN has been trained on a set of 55 proteins, searching for a relation between protein fragments modeled by 13alpha torsion angles and the residue corresponding to the central alpha torsion angle of the fragment. The results obtained show that only Asp, Gly, Pro, Ser and Val residues are often a necessary, even though not sufficient, condition to obtain a specific folded fragment structure, playing therefore, the role of "key residue" of this fragment.
PubMed: 16689212
Affiliations:
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Le document en format XML
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This approach, that can be regarded as an inverse protein folding problem, investigates whether and when a protein fragment needs a specific residue in the center of its primary structure as a necessary condition to fold as observed. To perform this analysis, an ANN has been trained on a set of 55 proteins, searching for a relation between protein fragments modeled by 13alpha torsion angles and the residue corresponding to the central alpha torsion angle of the fragment. The results obtained show that only Asp, Gly, Pro, Ser and Val residues are often a necessary, even though not sufficient, condition to obtain a specific folded fragment structure, playing therefore, the role of "key residue" of this fragment.</div></front></TEI><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Ruggiero, Carmelina" sort="Ruggiero, Carmelina" uniqKey="Ruggiero C" first="Carmelina" last="Ruggiero">Carmelina Ruggiero</name></noCountry><country name="Italie"><noRegion><name sortKey="Sacile, Roberto" sort="Sacile, Roberto" uniqKey="Sacile R" first="Roberto" last="Sacile">Roberto Sacile</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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