Understanding the role of the topology in protein folding by computational inverse folding experiments. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Understanding the role of the topology in protein folding by computational inverse folding experiments. (Articolo in rivista) (literal)

Anno

• 2008-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.compbiolchem.2008.03.015 (literal)

Alternative label

• Mucherino A, Costantini S, di Serafino D, D'Apuzzo M, Facchiano A, Colonna G (2008)
  Understanding the role of the topology in protein folding by computational inverse folding experiments.
  in Computational biology and chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Mucherino A, Costantini S, di Serafino D, D'Apuzzo M, Facchiano A, Colonna G (literal)

Pagina inizio

• 223 (literal)

Pagina fine

• 239 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni

• 0 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 32 (literal)

Rivista

• Computational biology and chemistry (Rivista)

Note

• PubMe (literal)
• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Seconda Università di Napoli Istituto di Scienze dell'Alimentazione, CNR, Avellino (literal)

Titolo

• Understanding the role of the topology in protein folding by computational inverse folding experiments. (literal)

Abstract

• Recent studies suggest that protein folding should be revisited as the emergent property of a complex system and that the nature allows only a very limited number of folds that seem to be strongly influenced by geometrical properties. In this work we explore the principles underlying this new view and show how helical protein conformations can be obtained starting from simple geometric considerations. We generated a large data set of C-alpha traces made of 65 points, by computationally solving a backbone model that takes into account only topological features of the all-alpha proteins; then, we built corresponding tertiary structures, by using the sequences associated to the crystallographic structures of four small globular all-alpha proteins from PDB, and analysed them in terms of structural and energetic properties. In this way we obtained four poorly populated sets of structures that are reasonably similar to the conformational states typical of the experimental PDB structures. These results show that our computational approach can capture the native topology of all-alpha proteins; furthermore, it generates backbone folds without the influence of the side chains and uses the protein sequence to select a specific fold among the generated folds. This agrees with the recent view that the backbone plays an important role in the protein folding process and that the amino acid sequence chooses its own fold within a limited total number of folds. (literal)

Prodotto di

• Institute of food sciences (ISA) (Istituto)
• Bioinformatica per lo studio di patologie umane, intolleranze alimentari e sicurezza alimentare (INT.P02.006.001) (Modulo)
• Metodologie di Spettrometria di Massa, Proteomica, Metabolomica e Bioinformatica nelle Scienze dell'Alimentazione (AG.P05.003.001) (Modulo)

Autore CNR

• ANGELO FACCHIANO (Unità di personale interno)
• SUSAN COSTANTINI (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of food sciences (ISA) (Istituto)
• Bioinformatica per lo studio di patologie umane, intolleranze alimentari e sicurezza alimentare (INT.P02.006.001) (Modulo)
• Metodologie di Spettrometria di Massa, Proteomica, Metabolomica e Bioinformatica nelle Scienze dell'Alimentazione (AG.P05.003.001) (Modulo)

Autore CNR di

• ANGELO FACCHIANO (Unità di personale interno)
• SUSAN COSTANTINI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Computational biology and chemistry (Rivista)