Home |  English version |  Mappa |  Commenti |  Sondaggio |  Staff |  Contattaci Cerca nel sito  
Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2008

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Understanding the role of the topology in protein folding by computational inverse folding experiments.

Anno di pubblicazione: 2008

Autori: Mucherino A, Costantini S, di Serafino D, D'Apuzzo M, Facchiano A, Colonna G

Affiliazioni autori: Seconda UniversitÓ di Napoli Istituto di Scienze dell'Alimentazione, CNR, Avellino

Autori CNR:

  • SUSAN COSTANTINI
  • ANGELO FACCHIANO

Lingua: inglese

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.

Lingua abstract: inglese

Pagine da: 223

Pagine a: 239

Rivista:

Computational biology and chemistry Elsevier,
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 1476-9271

Numero volume: 32

DOI: 10.1016/j.compbiolchem.2008.03.015

Indicizzato da:

  • ISI Web of Science (WOS) [WOS:000257981000001]
  • PubMed [18479970]

Altre informazioni: 0

Strutture CNR:

Moduli:

 
Torna indietro Richiedi modifiche Invia per email Stampa
Home Il CNR  |  I servizi News |   Eventi | Istituti |  Focus